Synopsis
The BioSAXS beamline is a highly automated beamline dedicated to the study of proteins, macromolecular complexes, viruses etc., in solution. Samples can be investigated under various conditions (temperature, buffer, pH, kinetics) in a high-throughput manner or a HPLC unit can be used for in-situ (online) purification.
Status:
open
Disciplines
- Life Sciences
- Chemistry
- Medicine
Applications
- Structural biology
- Pharmaceuticals
Techniques
-
BioSAXS - small-angle X-ray scattering (proteins/DNA)
-
SAXS - small-angle X-ray scattering
Beam size
- Minimum (H x V) : 50.0
x 50.0
µm²
-
Maximum (H x V) : 2.0
x 1.0
mm²
Sample environments
- Quartz capillary as a part of automated sample changer allowing temperature variations (from 4 to 60°C)
- HPLC (high performance liquid chromatography) system can be used in parallel with sample changer
Detectors
Pernot P., Theveneau P., Giraud T., Nogueira Fernandes R., Nurizzo D., Spruce D., Surr J., McSweeney S., Round A., Felisaz F., Foedinger L., Gobbo A., Huet J., Villard C. and Cipriani F., "New beamline dedicated to solution scattering from biological macromolecules at the ESRF", Journal of Physics: Conference Series 247 (2010) 012009-1-012009-8.
HadBD dehydratase from Mycobacterium tuberculosis fatty acid synthase type II: A singular structure for a unique function
Bories P., Rima J., Tranier S., Marcoux J., Grimoire Y., Tomaszczyk M., Launay A., Fata K., Marrakchi H., Burlet-Schiltz O., Mourey L., Ducoux-Petit M., Bardou F., Bon C., Quémard A.,
Protein Science 33, e4964-1-e4964-19 (2024)
Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus
Burmeister W.P., Boutin L., Balestra A.C., Gröger H., Ballandras-Colas A., Hutin S., Kraft C., Grimm C., Böttcher B., Fischer U., Tarbouriech N., Iseni F.,
PLoS Pathogens 20, e1011652-1-e1011652-22 (2024)
Comparison of the self-assembly and cytocompatibility of conjugates of Fmoc (9-fluorenylmethoxycarbonyl) with hydrophobic, aromatic, or charged amino acids
Castelletto V., De Mello L., Da Silva E.R., Seitsonen J., Hamley I.W.,
Journal of Peptide Science 30, e3571-1-e3571-10 (2024)
Molecular basis for different substrate-binding sites and chaperone functions of the BRICHOS domain
Chen G.F., Wang Y., Zheng Z.H., Jiang W.S., Leppert A., Zhong X.Y., Belorusova A., Siegal G., Jegerschöld C., Koeck P.J.B., Abelein A., Hebert H., Knight S.D., Johansson J.,
Protein Science 33, e5063-1-e5063-16 (2024)
SAXS/WAXS data of conformationally flexible ribose binding protein
Choudhury J., Yonezawa K., Anu A., Shimizu N., Chaudhuri B.,
Data in Brief 52, 109932-1-109932-7 (2024)
Towards natural care products: Structural and deposition studies of bio-based polymer and surfactant mixtures
Del Giudice A., Gubitosi M., Sthoer A., Köhler S., Ayscough S., Skoda M.W.A., Nylander T., Halthur T.,
Colloids and Surfaces A 698, 134365-1-134365-11 (2024)
Add this RSS feed to your favorite RSS reader (Thunderbird, Outlook etc...) or install an add-on to your browser, such as RSSPreview for Firefox