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.
Chameleonic amphiphile: The unique multiple self-assembly properties of a natural glycolipid in excess of water
Baccile N., Poirier A., Seyrig C., Le Griel P., Pérez J., Hermida-Merino D., Pernot P., Roelants S.L.K.W., Soetaert W.,
Journal of Colloid and Interface Science 630, 404-415 (2023)
Shear recovery and temperature stability of Ca2+ and Ag+ glycolipid fibrillar metallogels with unusual β-sheet-like domains
Poirier A., Le Griel P., Bizien T., Zinn T., Pernot P., Baccile N.,
Soft Matter , epub (2023)
Ca2+ and Ag+ orient low-molecular weight amphiphile self-assembly into “nano-fishnet” fibrillar hydrogels with unusual β-sheet-like raft domains
Poirier A., Le Griel P., Hoffmann I., Pérez J., Pernot P., Fresnais J., Baccile N.,
Soft Matter , epub (2023)
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex
Shukla A., Afsar M., Khanam T., Kumar N., Ali F., Kumar S., Jahan F., Ramachandran R.,
International Journal of Biological Macromolecules 225, 442-453 (2023)
Human 14-3-3 proteins site-selectively bind the mutational hotspot region of SARS-CoV-2 nucleoprotein modulating its phosphoregulation
Tugaeva K.V., Sysoeva A.A., Kapitonova A.A., Smith J.L.R., Zhu P., Cooley R.B., Antson A.A., Sluchanko N.N.,
Journal of Molecular Biology 435, 167891-1-167891-17 (2023)
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)
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