Publications

Publications describing MASSIF-1:

Please cite the appropriate references for experiments performed on MASSIF-1. An endnote library can be downloaded here

Svensson, O., Gilski, M., Nurizzo, D. & Bowler, M. W. (2018). Multi-position data collection and dynamic beam sizing: recent improvements to the automatic data-collection algorithms on MASSIF-1, Acta Cryst. D74, 433-440, http://dx.doi.org/10.1107/S2059798318003728

Describes the improvements made to the automatic data collection algorithms including dynamic adaptation of beam diameter to crystal volume and multi-position and helical data collection (MXPressP)

Svensson, O., Monaco, S., Popov, A. N., Nurizzo, D. & Bowler, M. W. (2015). The fully automatic characterization and data collection from crystals of biological macromolecules, Acta Cryst. D71, 1757-1767, http://dx.doi.org/10.1107/S1399004715011918

Describes the original developments in sample location, characterisation and data collection algorithms (automesh, X-ray centring, MXPressE and SAD data collection protocols etc.), should be cited for all experiments conducted on MASSIF-1 and those using X-ray centring

Bowler M.W., Nurizzo, D., Barrett, R., Beteva, A., Bodin, M., Caserotto, H., Delageniere, S., Dobias, F., Flot, D., Giraud, T., Guichard, N., Guijarro, M., Lentini, M., Leonard, G., McSweeney, S., Oskarsson, M., Schmidt, W., Snigirev, A., von Stetten, D., Surr, J., Svensson, O., Theveneau, P. and Mueller-Dieckmann, C. (2015) MASSIF-1: A beamline dedicated to the fully automatic characterisation and data collection from crystals of biological macromolecules J. Sync. Rad. 22 1540-1547 http://dx.doi.org/10.1107/S1600577515016604.

Describes the technical layout of the beamline, should be cited for all experiments conducted on MASSIF-1

Bowler, M.W., Svensson, O. & Nurizzo, D. (2016): Fully automatic macromolecular crystallography: the impact of MASSIF-1 on the optimum acquisition and quality of data, Cryst. Rev., 22, 233–249 http://dx.doi.org/10.1080/0889311X.2016.1155050.

Describes the first full year of operation of MASSIF-1, analysing the results from the large scale automation of MX data collection showing the advantages of fully autonomous data collection

Nurizzo, D., Bowler M.W., Caserotto, H., Dobias, F., Giraud, T., Surr, J., Guichard, N., Papp, G., Guijarro, M., Mueller-Dieckmann, C., Flot, D., McSweeney, S. Cipriani, F, Theveneau, P. and Leonard, G. (2016) RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments Acta Cryst D 72, 966-975, http://dx.doi.org/10.1107/S205979831601158X.

Describes the core robotic automation of the beamline

Svensson, O., Gilski, M., Nurizzo, D. & Bowler, M. W. (2019) A comparative anatomy of protein crystals: lessons from the automatic processing of 56,000 samples IUCrJ 6, 822-831 https://doi.org/10.1107/S2052252519008017

Describes the analysis of all the samples that have been sent to the beamline so far

Hutin, S., Van Laer, B., Mueller-Dieckmann, C., Leonard, G., Nurizzo, D., Bowler, M. W. (2019). Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules. J. Vis. Exp. 145, e59032, doi:10.3791/59032

A video article describing how to set up an experiment on the beamline

Publications that used data collected at MASSIF-1:

2021

190. Abdul Rehman, S. A., Armstrong, L. A., Lange, S. M., Kristariyanto, Y. A., Gräwert, T. W., Knebel, A., Svergun, D. I. & Kulathu, Y. (2021). Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2, Molecular Cell. https://doi.org/10.1016/j.molcel.2021.08.024

189. Eron, S. J., Huang, H., Agafonov, R. V., Fitzgerald, M. E., Patel, J., Michael, R. E., Lee, T. D., Hart, A. A., Shaulsky, J., Nasveschuk, C. G., Phillips, A. J., Fisher, S. L. & Good, A. (2021). Structural Characterization of Degrader-Induced Ternary Complexes Using Hydrogen–Deuterium Exchange Mass Spectrometry and Computational Modeling: Implications for Structure-Based Design, ACS Chemical Biology. https://pubs.acs.org/doi/10.1021/acschembio.1c00376

188. Bullen, G., Galson, J. D., Hall, G., Villar, P., Moreels, L., Ledsgaard, L., Mattiuzzo, G., Bentley, E. M., Masters, E. W., Tang, D., Millett, S., Tongue, D., Brown, R., Diamantopoulos, I., Parthiban, K., Tebbutt, C., Leah, R., Chaitanya, K., Ergueta-Carballo, S., Pazeraitis, D., Surade, S. B., Ashiru, O., Crippa, L., Cowan, R., Bowler, M. W., Campbell, J. I., Lee, W.-Y. J., Carr, M. D., Matthews, D., Pfeffer, P., Hufton, S. E., Sawmynaden, K., Osbourn, J., McCafferty, J. & Karatt-Vellatt, A. (2021). Cross-Reactive SARS-CoV-2 Neutralizing Antibodies From Deep Mining of Early Patient Responses, Frontiers in Immunology 12. https://doi.org/10.3389/fimmu.2021.678570

187. Gemenetzi, K., Psomopoulos, F., Carriles, A. A., Gounari, M., Minici, C., Plevova, K., Sutton, L.-A., Tsagiopoulou, M., Baliakas, P., Pasentsis, K., Anagnostopoulos, A., Sandaltzopoulos, R., Rosenquist, R., Davi, F., Pospisilova, S., Ghia, P., Stamatopoulos, K., Degano, M. & Chatzidimitriou, A. (2021). Higher-order immunoglobulin repertoire restrictions in CLL: the illustrative case of stereotyped subsets 2 and 169, Blood 137, 1895-1904.

186. Clément, D. A., Leseigneur, C., Gelin, M., Coelho, D., Huteau, V., Lionne, C., Labesse, G., Dussurget, O. & Pochet, S. (2020). New Chemical Probe Targeting Bacterial NAD Kinase, Molecules 25, 4893.

185. Veerman, J. J. N., Bruseker, Y. B., Damen, E., Heijne, E. H., van Bruggen, W., Hekking, K. F. W., Winkel, R., Hupp, C. D., Keefe, A. D., Liu, J., Thomson, H. A., Zhang, Y., Cuozzo, J. W., McRiner, A. J., Mulvihill, M. J., van Rijnsbergen, P., Zech, B., Renzetti, L. M., Babiss, L. & Müller, G. (2021). Discovery of 2,4-1H-Imidazole Carboxamides as Potent and Selective TAK1 Inhibitors, ACS Medicinal Chemistry Letters. https://pubs.acs.org/doi/10.1021/acsmedchemlett.0c00547

184. Voegele, A., Sadi, M., O'Brien, D. P., Gehan, P., Raoux-Barbot, D., Davi, M., Hoos, S., Brûlé, S., Raynal, B., Weber, P., Mechaly, A., Haouz, A., Rodriguez, N., Vachette, P., Durand, D., Brier, S., Ladant, D. & Chenal, A. A High-Affinity Calmodulin-Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells, Advanced Science, 2003630. https://doi.org/10.1002/advs.202003630

183. Bellin, L., Del Caño-Ochoa, F., Velázquez-Campoy, A., Möhlmann, T. & Ramón-Maiques, S. (2021). Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase, Nature Communications 12, 947. https://doi.org/10.1038/s41467-021-21165-9

182. Du, J., Wrisberg, M.-K. v., Gulen, B., Stahl, M., Pett, C., Hedberg, C., Lang, K., Schneider, S. & Itzen, A. (2021). Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1, Nature Communications 12, 460. https://doi.org/10.1038/s41467-020-20702-2

181. Varaksa, T., Bukhdruker, S., Grabovec, I., Marin, E., Kavaleuski, A., Gusach, A., Kovalev, K., Maslov, I., Luginina, A., Zabelskii, D., Astashkin, R., Shevtsov, M., Smolskaya, S., Kavaleuskaya, A., Shabunya, P., Baranovsky, A., Dolgopalets, V., Charnou, Y., Savachka, A., Litvinovskaya, R., Hurski, A., Shevchenko, E., Rogachev, A., Mishin, A., Gordeliy, V., Gabrielian, A., Hurt, D. E., Nikonenko, B., Majorov, K., Apt, A., Rosenthal, A., Gilep, A., Borshchevskiy, V. & Strushkevich, N. (2021). Metabolic Fate of Human Immunoactive Sterols in Mycobacterium tuberculosis, Journal of Molecular Biology 433, 166763.

180. Delfosse, V., Huet, T., Harrus, D., Granell, M., Bourguet, M., Gardia-Parège, C., Chiavarina, B., Grimaldi, M., Le Mével, S., Blanc, P., Huang, D., Gruszczyk, J., Demeneix, B., Cianférani, S., Fini, J.-B., Balaguer, P. & Bourguet, W. (2021). Mechanistic insights into the synergistic activation of the RXR–PXR heterodimer by endocrine disruptor mixtures, Proceedings of the National Academy of Sciences 118, e2020551118.

2020

179. van Tilburg, G. B. A., Murachelli, A. G., Fish, A., van der Heden van Noort, G. J., Ovaa, H. & Sixma, T. K. (2020). K27-Linked Diubiquitin Inhibits UCHL3 via an Unusual Kinetic Trap, Cell Chemical Biology. https://doi.org/10.1016/j.chembiol.2020.11.005

178. Voutilainen, S., Heinonen, M., Andberg, M., Jokinen, E., Maaheimo, H., Pääkkönen, J., Hakulinen, N., Rouvinen, J., Lähdesmäki, H., Kaski, S., Rousu, J., Penttilä, M. & Koivula, A. (2020). Substrate specificity of 2-deoxy-D-ribose 5-phosphate aldolase (DERA) assessed by different protein engineering and machine learning methods, Applied Microbiology and Biotechnology 104, 10515-10529.

177. Beyer, H. M., Virtanen, S. I., Aranko, A. S., Mikula, K. M., Lountos, G. T., Wlodawer, A., Ollila, O. H. S. & Iwaï, H. (2020). The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms, International Journal of Molecular Sciences 21, 8367.

176. Liess, A. K. L., Kucerova, A., Schweimer, K., Schlesinger, D., Dybkov, O., Urlaub, H., Mansfeld, J. & Lorenz, S. (2020). Dimerization regulates the human APC/C-associated ubiquitin-conjugating enzyme UBE2S, Science Signaling 13, eaba8208.

175. Münzker, L., Petrick, J. K., Schleberger, C., Clavel, D., Cornaciu, I., Wilcken, R., Márquez, J. A., Klebe, G., Marzinzik, A. & Jahnke, W. (2020). Fragment-Based Discovery of Non-bisphosphonate Binders of Trypanosoma brucei Farnesyl Pyrophosphate Synthase, Chembiochem : a European journal of chemical biology. https://doi.org/10.1002/cbic.202000246

174. Ausar, S. F., Zhu, S., Duprez, J., Cohen, M., Bertrand, T., Steier, V., Wilson, D. J., Li, S., Sheung, A., Brookes, R. H., Pedyczak, A., Rak, A. & Andrew James, D. (2020). Genetically detoxified pertussis toxin displays near identical structure to its wild-type and exhibits robust immunogenicity, Communications Biology 3, 427.

173. Martinelli, L., Adamopoulos, A., Johansson, P., Wan, P. T., Gunnarsson, J., Guo, H., Boyd, H., Zelcer, N. & Sixma, T. K. (2020). Structural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate binding site, Journal of Biological Chemistry. https://doi.org/10.1074/jbc.RA120.014349

172. Waaler, J., Leenders, R. G. G., Sowa, S. T., Alam Brinch, S., Lycke, M., Nieczypor, P., Aertssen, S., Murthy, S., Galera-Prat, A., Damen, E., Wegert, A., Nazaré, M., Lehtiö, L. & Krauss, S. (2020). Preclinical Lead Optimization of a 1,2,4-Triazole Based Tankyrase Inhibitor, Journal of Medicinal Chemistry 63, 6834-6846.

171. Münzker, L., Petrick, J., Schleberger, C., Clavel, D., Cornaciu, I., Wilcken, R., Márquez, J. A., Klebe, G., Marzinzik, A. & Jahnke, W. Fragment-based discovery of non-bisphosphonate binders of Trypanosoma brucei farnesyl pyrophosphate synthase, ChemBioChem https://doi.org/10.1002/cbic.202000246

170. Lee, Y., Warne, T., Nehmé, R., Pandey, S., Dwivedi-Agnihotri, H., Chaturvedi, M., Edwards, P. C., García-Nafría, J., Leslie, A. G. W., Shukla, A. K. & Tate, C. G. (2020). Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor, Nature. https://doi.org/10.1038/s41586-020-2419-1

169. Stutz, C. & Blein, S. (2020). A single mutation increases heavy chain heterodimer assembly of bispecific antibodies by inducing structural disorder in one homodimer species, Journal of Biological Chemistry. https://doi.org/10.1074/jbc.RA119.012335

168. Mais, C.-N., Hermann, L., Altegoer, F., Seubert, A., Richter, A. A., Wernersbach, I., Czech, L., Bremer, E. & Bange, G. (2020). Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase–deacetylase complex, Journal of Biological Chemistry. https://doi.org/10.1074/jbc.RA120.012722

167. Altegoer, F., Weiland, P., Giammarinaro, P. I., Freibert, S.-A., Binnebesel, L., Han, X., Lepak, A., Kahmann, R., Lechner, M. & Bange, G. (2020). The two paralogous kiwellin proteins KWL1 and KWL1-b from maize are structurally related and have overlapping functions in plant defense, Journal of Biological Chemistry 295, 7816-7825.

166. Bellenie, B. R., Cheung, K.-M. J., Varela, A., Pierrat, O. A., Collie, G. W., Box, G. M., Bright, M. D., Gowan, S., Hayes, A., Rodrigues, M. J., Shetty, K. N., Carter, M., Davis, O. A., Henley, A. T., Innocenti, P., Johnson, L. D., Liu, M., de Klerk, S., Le Bihan, Y.-V., Lloyd, M. G., McAndrew, P. C., Shehu, E., Talbot, R., Woodward, H. L., Burke, R., Kirkin, V., van Montfort, R. L. M., Raynaud, F. I., Rossanese, O. W. & Hoelder, S. (2020). Achieving In Vivo Target Depletion through the Discovery and Optimization of Benzimidazolone BCL6 Degraders, Journal of Medicinal Chemistry 63, 4047-4068.

165. Dalle Vedove, A., Zonta, F., Zanforlin, E., Demitri, N., Ribaudo, G., Cazzanelli, G., Ongaro, A., Sarno, S., Zagotto, G., Battistutta, R., Ruzzene, M. & Lolli, G. (2020). A novel class of selective CK2 inhibitors targeting its open hinge conformation, European Journal of Medicinal Chemistry 195, 112267.

164. Khan, F., Kurre, D. & Suguna, K. (2020). Crystal structures of a β-trefoil lectin from Entamoeba histolytica in monomeric and a novel disulfide bond-mediated dimeric forms, Glycobiology 30, 474-488.

163. Dian, C., Pérez-Dorado, I., Rivière, F., Asensio, T., Legrand, P., Ritzefeld, M., Shen, M., Cota, E., Meinnel, T., Tate, E. W. & Giglione, C. (2020). High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation, Nature Communications 11, 1132.

162. Gunnell, E. A., Al-Noori, A., Muhsen, U., Davies, C. C., Dowden, J. & Dreveny, I. (2020). Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4), Biochemical Journal 477, 787-800.

161. Ashok, Y., Maksimainen, M. M., Kallio, T., Kilpeläinen, P. & Lehtiö, L. (2020). FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici, PLOS ONE 15, e0223870.

160. Henley, Z. A., Amour, A., Barton, N., Bantscheff, M., Bergamini, G., Bertrand, S. M., Convery, M., Down, K., Dümpelfeld, B., Edwards, C. D., Grandi, P., Gore, P. M., Keeling, S., Livia, S., Mallett, D., Maxwell, A., Price, M., Rau, C., Reinhard, F. B. M., Rowedder, J., Rowland, P., Taylor, J. A., Thomas, D. A., Hessel, E. M. & Hamblin, J. N. (2020). Optimization of Orally Bioavailable PI3Kδ Inhibitors and Identification of Vps34 as a Key Selectivity Target, Journal of Medicinal Chemistry 63, 638-655.

161. Gelin, M., Paoletti, J., Nahori, M.-A., Huteau, V., Leseigneur, C., Jouvion, G., Dugué, L., Clément, D., Pons, J.-L., Assairi, L., Pochet, S., Labesse, G. & Dussurget, O. (2020). From Substrate to Fragments to Inhibitor Active In Vivo against Staphylococcus aureus, ACS Infectious Diseases. https://doi.org/10.1021/acsinfecdis.9b00368

160. Muir, K. W., Li, Y., Weis, F. & Panne, D. (2020). The structure of the cohesin ATPase elucidates the mechanism of SMC–kleisin ring opening, Nature Structural & Molecular Biology. https://doi.org/10.1038/s41594-020-0379-7

159. Alexander K.H. Weiss, Andreas Naschberger, Elia Cappuccio, Christina Metzger, Lorenza Mottes, Max Holzknecht, Jill von Velsen, Matthew W. Bowler, Bernhard Rupp, Pidder Jansen-Dürr, Structural and Functional Comparison of Fumarylacetoacetate Domain Containing Protein 1 (FAHD1) in Human and Mouse Biosci Rep BSR20194431. doi: https://doi.org/10.1042/BSR20194431

158. Lai, X., Wichers, H. J., Soler-Lopez, M. & Dijkstra, B. W. (2020). Phenylthiourea Binding to Human Tyrosinase-Related Protein 1, International Journal of Molecular Sciences 21, 915.

157. Liu, B., Trout, R. E. L., Chu, G.-H., McGarry, D., Jackson, R. W., Hamrick, J. C., Daigle, D. M., Cusick, S. M., Pozzi, C., De Luca, F., Benvenuti, M., Mangani, S., Docquier, J.-D., Weiss, W. J., Pevear, D. C., Xerri, L. & Burns, C. J. (2019). Discovery of Taniborbactam (VNRX-5133): A Broad-Spectrum Serine- and Metallo-β-lactamase Inhibitor for Carbapenem-Resistant Bacterial Infections, Journal of Medicinal Chemistry.

156. Li, Y., Haarhuis, J. H. I., Cacciatore, Á. S., Oldenkamp, R., van Ruiten, M. S., Willems, L., Teunissen, H., Muir, K. W., de Wit, E., Rowland, B. D. & Panne, D. (2020). The structural basis for cohesin–CTCF-anchored loops, Nature. https://doi.org/10.1038/s41586-019-1910-z

2019

155. Chaugule, V. K., Arkinson, C., Rennie, M. L., Kämäräinen, O., Toth, R. & Walden, H. (2019). Allosteric mechanism for site-specific ubiquitination of FANCD2, Nature Chemical Biology. https://doi.org/10.1038/s41589-019-0426-z

154. Nicoll, C. R., Bailleul, G., Fiorentini, F., Mascotti, M. L., Fraaije, M. W. & Mattevi, A. (2019). Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs, Nature Structural & Molecular Biology. https://doi.org/10.1038/s41594-019-0347-2

153. Lefranc, J., Schulze, V. K., Hillig, R. C., Briem, H., Prinz, F., Mengel, A., Heinrich, T., Bálint, J., Rengachari, S., Irlbacher, H., Stöckigt, D., Bömer, U., Bader, B., Gradl, S. N., Nising, C. F., von Nussbaum, F., Mumberg, D., Panne, D. & Wengner, A. (2019). Discovery of BAY-985 a highly selective TBK1/Ikkε inhibitor, Journal of Medicinal Chemistry. http://doi.org/10.1021/acs.jmedchem.9b01460

152. Trstenjak, N., Milić, D., Graewert, M. A., Rouha, H., Svergun, D., Djinović-Carugo, K., Nagy, E. & Badarau, A. (2019). Molecular mechanism of leukocidin GH–integrin CD11b/CD18 recognition and species specificity, Proceedings of the National Academy of Sciences 201913690.

151. Naschberger, A., Juyoux, P., von Velsen, J., Rupp, B. & Bowler, M. W. (2019). Controlled dehydration, structural flexibility and gadolinium MRI contrast compound binding in the human plasma glycoprotein afamin, Acta Cryst. D 75, 1071-1083.

150. Banerjee, P., Chanchal & Jain, D. (2019). Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition in Pseudomonas aeruginosa, ACS Chemical Biology 14, 1515-1527.

149. Grobben, Y., Uitdehaag, J. C. M., Willemsen-Seegers, N., Tabak, W. W. A., Man, J. d., Buijsman, R. C. & Zaman, G. J. R. (2019). Structural insights into human Arginase-1 pH dependence and its inhibition by the small molecule inhibitor CB-1158, Journal of Structural Biology: X 100014.

148. Drulyte, I., Obajdin, J., Trinh, C. H., Kalverda, A. P., van der Kamp, M. W., Hemsworth, G. R. & Berry, A. (2019). Crystal structure of the putative cyclase IdmH from the indanomycin nonribosomal peptide synthase/polyketide synthase, IUCrJ 6. https://doi.org/10.1107/S2052252519012399

147. de Groot, A., et al., Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus. (2019), Nucleic Acids Research. https://doi.org/10.1093/nar/gkz883

146. Cassotta, A., Mikol, V., Bertrand, T., Pouzieux, S., Le Parc, J., Ferrari, P., Dumas, J., Auer, M., Deisenhammer, F., Gastaldi, M., Franciotta, D., Silacci-Fregni, C., Fernandez Rodriguez, B., Giacchetto-Sasselli, I., Foglierini, M., Jarrossay, D., Geiger, R., Sallusto, F., Lanzavecchia, A. & Piccoli, L. (2019). A single T cell epitope drives the neutralizing anti-drug antibody response to natalizumab in multiple sclerosis patients, Nature Medicine 25, 1402-1407.

145. Ohayon, D., De Chiara, A., Dang, P. M.-C., Thieblemont, N., Chatfield, S., Marzaioli, V., Burgener, S. S., Mocek, J., Candalh, C., Pintard, C., Tacnet-Delorme, P., Renault, G., Lagoutte, I., Favier, M., Walker, F., Hurtado-Nedelec, M., Desplancq, D., Weiss, E., Benarafa, C., Housset, D., Marie, J.-C., Frachet, P., El-Benna, J. & Witko-Sarsat, V. (2019). Cytosolic PCNA interacts with p47phox and controls NADPH oxidase NOX2 activation in neutrophils, The Journal of Experimental Medicine jem.20180371.

144. Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F., Morlot, C., Abian, O., Gutsche, I., Velazquez-Campoy, A., Schanda, P. & Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors, Science Advances 5, eaaw3818.

143. Banerjee, P., Chanchal & Jain, D. (2019). Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition in Pseudomonas aeruginosa, ACS Chemical Biology 14, 1515-1527.

142. Wang, H., Schoebel, S., Schmitz, F., Dong, H. & Hedfalk, K. (2019). Characterization of aquaporin-driven hydrogen peroxide transport, Biochimica et Biophysica Acta (BBA) - Biomembranes 183065.

141. Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F., Morlot, C., Abian, O., Gutsche, I., Velazquez-Campoy, A., Schanda, P. & Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors, Science Advances 5, eaaw3818.

140. Medve, L., Achilli, S., Guzman-Caldentey, J., Thépaut, M., Senaldi, L., Le Roy, A., Sattin, S., Ebel, C., Vivès, C., Martin-Santamaria, S., Bernardi, A. & Fieschi, F. Enhancing potency and selectivity of a DC-SIGN glycomimetic ligand by fragment-based design: structural basis, Chemistry – A European Journal https://doi.org/10.1002/chem.201903391

139. Kersten, C., Fleischer, E., Kehrein, J., Borek, C., Jaenicke, E., Sotriffer, C. & Brenk, R. (2019). How To Design Selective Ligands for Highly Conserved Binding Sites: A Case Study Using N-Myristoyltransferases as a Model System, Journal of Medicinal Chemistry https://pubs.acs.org/doi/10.1021/acs.jmedchem.9b00586

138. Biterova, E. I., Isupov, M. N., Keegan, R. M., Lebedev, A. A., Sohail, A. A., Liaqat, I., Alanen, H. I. & Ruddock, L. W. (2019). The crystal structure of human microsomal triglyceride transfer protein, Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.1903029116

137. Hassler, M., Shaltiel, I. A., Kschonsak, M., Simon, B., Merkel, F., Thärichen, L., Bailey, H. J., Macošek, J., Bravo, S., Metz, J., Hennig, J. & Haering, C. H. (2019). Structural Basis of an Asymmetric Condensin ATPase Cycle, Molecular Cell 74, 1175-1188.e1179.

136. Thouennon, E., Delfosse, V., Bailly, R., Blanc, P., Boulahtouf, A., Grimaldi, M., Barducci, A., Bourguet, W. & Balaguer, P. (2019). Insights into the activation mechanism of human estrogen-related receptor γ by environmental endocrine disruptors, Cellular and Molecular Life Sciences.

135. Kumar, R., Oliver, C., Brun, C., Juarez-Martinez, A. B., Tarabay, Y., Kadlec, J. & de Massy, B. (2018). Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4, Life Science Alliance 1, e201800259.

134. Adamopoulos, A., Landskron, L., Heidebrecht, T., Tsakou, F., Bleijerveld, O. B., Altelaar, M., Nieuwenhuis, J., Celie, P. H. N., Brummelkamp, T. R. & Perrakis, A. (2019). Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP, Nature Structural & Molecular Biology 26, 567-570.

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49. Roversi, P., Marti, L., Caputo, A. T., Alonzi, D. S., Hill, J. C., Dent, K. C., Kumar, A., Levasseur, M. D., Lia, A., Waksman, T., Basu, S., Soto Albrecht, Y., Qian, K., McIvor, J. P., Lipp, C. B., Siliqi, D., Vasiljević, S., Mohammed, S., Lukacik, P., Walsh, M. A., Santino, A. & Zitzmann, N. (2017). Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint, Proceedings of the National Academy of Sciences. 10.1073/pnas.1703682114

48. Hiruma, Y., Koch, A., Hazraty, N., Tsakou, F., Medema, R. H., Joosten, R. P. & Perrakis, A. (2017). Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures, J. Biol. Chem. 10.1074/jbc.M117.783555

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45. Jonnalagadda, S.V.R., Ornithopoulou, E., Orr, A., Mossou, E., Forsyth, T., Mitchell, E.P., Bowler, M.W., Mitraki, A. and Tamamis, P. (2017) Computational Design of Amyloid Self-Assembling Peptides Bearing Aromatic Residues and the Cell Adhesive Motif Arg-Gly-Asp Mol. Syst. Des. Eng., 10.1039/C7ME00016B

44. Lai, X., Wichers, H. J., Soler-Lopez, M. & Dijkstra, B. W. (2017) Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis, Angewandte Chemie International Edition

43. Handramouli, S., Malito, E., Nguyen, T., Luisi, K., Donnarumma, D., Xing, Y., Norais, N., Yu, D. and Carfi, A. (2017) Structural basis for potent antibody-mediated neutralization of human cytomegalovirus, Science Immunology, 2, 10.1126/sciimmunol.aan1457

42. Hutchinson, J. P., Rowland, P., Taylor, M. R. D., Christodoulou, E. M., Haslam, C., Hobbs, C. I., Holmes, D. S., Homes, P., Liddle, J., Mole, D. J., Uings, I., Walker, A. L., Webster, S. P., Mowat, C. G. & Chung, C.-w. (2017). Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase, Nature communications 8, 15827.

41. Bezerra, G. A., Ohara-Nemoto, Y., Cornaciu, I., Fedosyuk, S., Hoffmann, G., Round, A., Márquez, J. A., Nemoto, T. K. & Djinović-Carugo, K. (2017). Bacterial protease uses distinct thermodynamic signatures for substrate recognition, Scientific Reports 7, 2848.

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38. Uitdehaag, J. C. M., de Man, J., Willemsen-Seegers, N., Prinsen, M. B. W., Libouban, M. A. A., Sterrenburg, J. G., de Wit, J. J. P., de Vetter, J. R. F., de Roos, J. A. D. M., Buijsman, R. C. & Zaman, G. J. R. (2017). Target Residence Time-Guided Optimization on TTK Kinase Results in Inhibitors with Potent Anti-Proliferative Activity, Journal of Molecular Biology 429, 2211-2230.

37. Pellegrini, E., Signor, L., Singh, S., Boeri Erba, E. & Cusack, S. (2017). Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation, PLOS ONE 12, e0177161

36. Frandsen, K. E. H., Poulsen, J.-C. N., Tandrup, T. & Lo Leggio, L. Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH, Carbohydrate Research.

35. Carboni, F., Adamo, R., Fabbrini, M., De Ricco, R., Cattaneo, V., Brogioni, B., Veggi, D., Pinto, V., Passalacqua, I., Oldrini, D., Rappuoli, R., Malito, E., Margarit, I. y. R. & Berti, F. (2017). Structure of a protective epitope of group B Streptococcus type III capsular polysaccharide, Proceedings of the National Academy of Sciences 114, 5017-5022.

34. Skjoldager, N., Blanner Bang, M., Rykær, M., Björnberg, O., Davies, M. J., Svensson, B., Harris, P. & Hägglund, P. (2017). The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage, Scientific Reports 7, 46282.

33. Sander, B., Xu, W., Eilers, M., Popov, N. & Lorenz, S. (2017). A conformational switch regulates the ubiquitin ligase HUWE1, eLife 6, e21036.

32. Cao, L., Cantos-Fernandes, S. & Gigant, B. (2017). The structural switch of nucleotide-free kinesin, Scientific Reports 7, 42558.

31. Fernández, I., Cornaciu, I., Carrica, M. d. C., Uchikawa, E., Hoffmann, G., Sieira, R., Márquez, J. A. & Goldbaum, F. A. (2017). Three-Dimensional Structure of Full-Length NtrX, an Unusual Member of the NtrC Family of Response Regulators, Journal of Molecular Biology 429, 1192-1212.

30. Cheeseman, M. D., Chessum, N. E. A., Rye, C. S., Pasqua, A. E., Tucker, M. J., Wilding, B., Evans, L. E., Lepri, S., Richards, M., Sharp, S. Y., Ali, S., Rowlands, M., O’Fee, L., Miah, A., Hayes, A., Henley, A. T., Powers, M., te Poele, R., De Billy, E., Pellegrino, L., Raynaud, F., Burke, R., van Montfort, R. L. M., Eccles, S. A., Workman, P. & Jones, K. (2017). Discovery of a Chemical Probe Bisamide (CCT251236): An Orally Bioavailable Efficacious Pirin Ligand from a Heat Shock Transcription Factor 1 (HSF1) Phenotypic Screen, Journal of Medicinal Chemistry 60, 180-201.

29. Košak, U., Knez, D., Coquelle, N., Brus, B., Pišlar, A., Nachon, F., Brazzolotto, X., Kos, J., Colletier, J.-P. & Gobec, S. (2017). N-Propargylpiperidines with naphthalene-2-carboxamide or naphthalene-2-sulfonamide moieties: Potential multifunctional anti-Alzheimer’s agents, Bioorganic & Medicinal Chemistry 25, 633-645.

28. Kristariyanto, Y. A., Abdul Rehman, S. A., Weidlich, S., Knebel, A. & Kulathu, Y. (2017). A single MIU motif of MINDY‐1 recognizes K48‐linked polyubiquitin chains, EMBO reports 18, 392-402.

27. Na, Z., Yeo, S. P., Bharath, S. R., Bowler, M. W., Balikci, E., Wang, C.-I. & Song, H. (2017). Structural basis for blocking PD-1-mediated immune suppression by therapeutic antibody pembrolizumab, Cell Res 27, 147-150.

2016

26. Varshney, D., Petit, A.-P., Bueren-Calabuig, J. A., Jansen, C., Fletcher, D. A., Peggie, M., Weidlich, S., Scullion, P., Pisliakov, A. V. & Cowling, V. H. (2016). Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM, Nucleic Acids Research 44, 10423-10436.

25. Fedosyuk, S., Bezerra, G. A., Radakovics, K., Smith, T. K., Sammito, M., Bobik, N., Round, A., Ten Eyck, L. F., Djinović-Carugo, K., Usón, I. & Skern, T. (2016). Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins, PLOS Pathogens 12, e1006079.

24. Perveen, S., Rashid, N. & Papageorgiou, A. C. (2016). Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis, Acta Crystallographica Section F 72, 804-812.

23. Gógl, G., Alexa, A., Kiss, B., Katona, G., Kovács, M., Bodor, A., Reményi, A. & Nyitray, L. (2016). Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY, Journal of Biological Chemistry 291, 11-27.

22. Altegoer, F., Rensing, S. A. & Bange, G. (2016). Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein, Proceedings of the National Academy of Sciences 113, 10168-10173

21. Volbeda, A., Darnault, C., Renoux, O., Reichmann, D., Amara, P., Ollagnier de Choudens, S. & Fontecilla-Camps, J. C. (2016). Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product, Journal of the American Chemical Society 138, 11802-11809

20. Kristensen, O., Kristensen, Lise B., Møllerud, S., Frydenvang, K., Pickering, Darryl S. & Kastrup, Jette S. (2016). The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate, Structure 24, 1582-1589.

19. Nuti, E., Cuffaro, D., D'Andrea, F., Rosalia, L., Tepshi, L., Fabbi, M., Carbotti, G., Ferrini, S., Santamaria, S., Camodeca, C., Ciccone, L., Orlandini, E., Nencetti, S., Stura, E. A., Dive, V. & Rossello, A. (2016). Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors, ChemMedChem 11, 1626-1637.

18. Borsari, C., Luciani, R., Pozzi, C., Poehner, I., Henrich, S., Trande, M., Cordeiro-da-Silva, A., Santarem, N., Baptista, C., Tait, A., Di Pisa, F., Dello Iacono, L., Landi, G., Gul, S., Wolf, M., Kuzikov, M., Ellinger, B., Reinshagen, J., Witt, G., Gribbon, P., Kohler, M., Keminer, O., Behrens, B., Costantino, L., Tejera Nevado, P., Bifeld, E., Eick, J., Clos, J., Torrado, J., Jiménez-Antón, M. D., Corral, M. J., Alunda, J. M., Pellati, F., Wade, R. C., Ferrari, S., Mangani, S. & Costi, M. P. (2016). Profiling of Flavonol Derivatives for the Development of Antitrypanosomatidic Drugs, Journal of Medicinal Chemistry 59, 7598-7616.

17. Caputo, A. T., Alonzi, D. S., Marti, L., Reca, I.-B., Kiappes, J. L., Struwe, W. B., Cross, A., Basu, S., Lowe, E. D., Darlot, B., Santino, A., Roversi, P. & Zitzmann, N. (2016). Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals, Proceedings of the National Academy of Sciences 113, E4630-E4638.

16. Hafstrand, I., Doorduijn, E.M., Duru, A.D., Buratto, J., Oliveira, C.C., Sandalova, T., van Hall, T., and Achour, A. (2016). The MHC Class I Cancer-Associated Neoepitope Trh4 Linked with Impaired Peptide Processing Induces a Unique Noncanonical TCR Conformer. The Journal of Immunology 196, 2327-2334.

15. Siitonen V, Selvaraj B, Niiranen L, Lindqvist Y, Schneider G, Metsä-Ketelä M (2016) Divergent non-heme iron enzymes in the nogalamycin biosynthetic pathway. Proc. Natl. Acad. Sci USA 113, 5251-5256

14. Zander U, Hoffmann G, Cornaciu I, Marquette J-P, Papp G, Landret C, Seroul G, Sinoir J, Rower M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Marquez JA (2016) Automated harvesting and processing of protein crystals through laser photoablation. Acta Cryst. D72, 454-466

13. Heggelund JE, Burschowsky D, Bjørnestad VA, Hodnik V, Anderluh G, Krengel U (2016) High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. PLoS Pathogens 12 : e1005567. doi:10.1371/journal.ppat.1005567

12. Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S (2016). Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains, Molecular Cell. 61, 125-37, doi:10.1016/j.molcel.2015.11.016

11. Muir K, Kschonsak M, Li Y, Metz J, Haering Christian H, Panne D (2016) Structure of the Pds5-Scc1 Complex and Implications for Cohesin Function. Cell reports 14, 2116-2126

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9. Forsberg Z, Nelson CE, Dalhus B, Mekasha S, Loose JS, Crouch LI, Rohr AK, Gardner JG, Eijsink VG, Vaaje-Kolstad G (2016) Structural and Functional Analysis of a Lytic Polysaccharide Monooxygenase Important for Efficient Utilization of Chitin in Cellvibrio japonicus. J. Biol. Chem 291, 7300-7312

8. Frandsen KEH, Simmons TJ, Dupree P, Poulsen J-CN, Hemsworth GR, Ciano L, Johnston EM, Tovborg M, Johansen KS, von Freiesleben P, Marmuse L, Fort S, Cottaz S, Driguez H, Henrissat B, Lenfant N, Tuna F, Baldansuren A, Davies GJ, Lo Leggio L, Walton PH (2016) The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nature Chemical Biology 12, 298-303

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6. Papageorgiou N, Lichiere J, Baklouti A, Ferron F, Sevajol M, Canard B, Coutard B (2016) Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. Acta Cryst. D72, 192-202

5. Mourier G, Salinas M, Kessler P, Stura EA, Leblanc M, Tepshi L, Besson T, Diochot S, Baron A, Douguet D, Lingueglia E, Servent D (2016) Mambalgin-1 Pain-relieving Peptide, Stepwise Solid-phase Synthesis, Crystal Structure, and Functional Domain for Acid-sensing Ion Channel 1a Inhibition. J. Biol. Chem 291, 2616-2629

2015

4. Marton, Z., Guillon, R., Krimm, I., Preeti, Rahimova, R., Egron, D., Jordheim, L.P., Aghajari, N., Dumontet, C., Périgaud, C., et al. (2015). Identification of Noncompetitive Inhibitors of Cytosolic 5′-Nucleotidase II Using a Fragment-Based Approach. Journal of Medicinal Chemistry 58, 9680-9696.

3. Koromyslova AD, Leuthold MM, Bowler MW, Hansman GS. (2015) The sweet quartet: Binding of fucose to the norovirus capsid. Virology 483, 203-208. doi: 10.1016/j.virol.2015.04.006

2. Pathak S, Alonso J, Schimpl M, Rafie K, Blair DE, Borodkin VS, Schuttelkopf AW, Albarbarawi O, van Aalten DMF (2015) The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nature Structural & Molecular Biology 22, 744-750

1. Kharde S, Calviño FR, Gumiero A, Wild K, Sinning I (2015). The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis, Nucleic Acids Res. 43, 7083–95, doi:10.1093/nar/gkv640

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