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.
An albumin unfolding and refolding cycle induced by a time-controlled pH jump
Del Giudice A., Del Giudice D., Spatola E., Alemanno V., Galantini L., Di Stefano S.,
Organic & Biomolecular Chemistry 23, 118-125 (2025)
Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies
Markússon S., Raasakka A., Schröder M., Sograte-Idrissi S., Rahimi A., Asadpour O., Korner H., Lodygin D., Eichel-Vogel Maria A., Chowdhury R., Sutinen A., Muruganandam G., Iyer M., Cooper Madeline H., Weigel Maya K., Ambiel N., Werner Hauke B., Zuchero J. Bradley, Opazo F., Kursula P.,
Journal of Neurochemistry 169, e16274-1-e16274-25 (2025)
Unveiling the crystal structure of thermostable dienelactone hydrolase exhibiting activity on terephthalate esters
Almeida D.V., Ciancaglini I., Hernandes Sandano A.L., Roman E.K.B., Brito Andrade V., Nunes A.B., Tramontina R., da Silva V.M., Gabel F., Corrêa T.L.R., Damasio A., Muniz J.R.C., Squina F.M., Garcia W.,
Enzyme and Microbial Technology 180, 110498-1-110498-10 (2024)
Biophysical analysis of the membrane-proximal Venus Flytrap domain of ESAG4 receptor-like adenylate cyclase from Trypanosoma brucei
Alves D.O., Geens R., da Silva Arruda H.R., Jennen L., Corthaut S., Wuyts E., Caldas de Andrade G., Prosdocimi F., Cordeiro Y., Pires J.R., Rezende Vieira L., de Oliveira G.A.P., Sterckx Y.G.J., Salmon D.,
Molecular and Biochemical Parasitology 260, 111653-1-111653-13 (2024)
An integrative structural study of the human full-length RAD52 at 2.2 Å resolution
Balboni B., Marotta R., Rinaldi F., Milordini G., Varignani G., Girotto S., Cavalli A.,
Communications Biology 7, 956-1-956-12 (2024)
Structural dynamics of the TPR domain of the peroxisomal cargo receptor Pex5 in Trypanosoma
Banasik M., Napolitano V., Blat A., Abdulkarim K., Plewka J., Czaplewski C., Gieldon A., Kozak M., Wladyka B., Popowicz G., Dubin G.,
International Journal of Biological Macromolecules 280, 135510-1-135510-9 (2024)
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