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.
A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host
Alexa A., Sok P., Gross F., Albert K., Kobori E., Póti A.L., Gógl G., Bento I., Kuang E., Taylor S.S., Zhu F., Ciliberto A., Reményi A.,
Nature Communications 13, 472-1-472-19 (2022)
Global fitting of multiple data frames from SEC-SAXS to investigate the structure of next-generation nanodiscs
Barclay A., Tidemand Johansen N., Gronbaek Tidemand F., Arleth L., Cramer Pedersen M.,
Acta Crystallographica D 78, 483-493 (2022)
Structural characterization of the full-length anti-CD20 antibody rituximab
Belviso B.D., Mangiatordi G.F., Alberga D., Mangini V., Carrozzini B., Caliandro R.,
Frontiers in Molecular Biosciences 9, 823174-1-823174-18 (2022)
The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a
Bessa L.M., Guseva S., Camacho-Zarco A.R., Salvi N., Maurin D., Mariño Pérez L., Botova M., Malki A., Nanao M., Ringkjøbing Jensen M., Ruigrok R.W.H., Blackledge M.,
Science Advances 8, eabm4034-1-eabm4034-12 (2022)
Development of a first-in-class small-molecule inhibitor of the C-terminal Hsp90 dimerization
Bhatia S., Spanier L., Bickel D., Dienstbier N., Woloschin V., Vogt M., Pols H., Lungerich B., Reiners J., Aghaallaei N., Diedrich D., Frieg B., Schliehe-Diecks J., Bopp B., Lang F., Gopalswamy M., Loschwitz J., Bajohgli B., Skokowa J., Borkhardt A., Hauer J., Hansen F.K., Smits S.H.J., Jose J., Gohlke H., Kurz T.,
ACS Central Science 8, 636-655 (2022)
Structural insights into highly similar spatial organization of zinc-finger associated domains with a very low sequence similarity
Bonchuk A.N., Boyko K.M., Nikolaeva A.Y., Burtseva A.D., Popov V.O., Georgiev P.G.,
Structure 30, 1004-1015 (2022)