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.
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)
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)
Diversifying de novo TIM barrels by hallucination
Beck J., Shanmugaratnam S., Höcker B.,
Protein Science 33, e5001-1-e5001-11 (2024)
Hindered intermolecular stacking of anti-parallel telomeric G-quadruplexes
Bertini L., Libera V., Catalini S., Schirò G., Orecchini A., Campanella R., Arciuolo V., Pagano B., Petrillo C., De Michele C., Comez L., Paciaroni A.,
Journal of Chemical Physics 161, 105101-1-105101-7 (2024)
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)
A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding
Botova M., Camacho-Zarco A.R., Tognetti J., Mamigonian Bessa L., Guseva S., Mikkola E., Salvi N., Maurin D., Herrmann T., Blackledge M.,
Science Advances 10, eaax2323-1-eaax2323-15 (2024)
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