New beamline dedicated to solution scattering from biological macromolecules at the ESRF

Pernot, Pétra; Théveneau, Pascal; Giraud, Thierry; Fernandes, R. N.; Nurizzo, Didier; Spruce, Darren; Surr, John; McSweeney, Seán; Round, Adam; Felisaz, Franck; Foedinger, L; Gobbo, Alexandre; Huet, Julien; Villard, C.; Cipriani, F.

doi:10.1088/1742-6596/247/1/012009

Cited by 86 publications

(88 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3 The small angle X-ray diffraction intensity I(s) multiplied by the square of the momentum transfer s, called a Kratky plot, as a function of the momentum transfer s of the tau protein at two different temperatures square of the scattering wave vector s 2 (i.e., s 2 I(s) versus s). The scattering profile for an unfolded state of a molecule falls off as 1/s at high values of the exchanged momentum s. The clearly defined surface of a folded protein leads to a scattering profile which falls off as 1/s 4 [46]. Therefore, the occurrence of a well-defined peak in the Kratky plot indicates that the molecule is in a compact state.…”

Section: Saxs Resultsmentioning

confidence: 98%

“…Tau entails no permanent secondary structures, and the aggregation in PHFs is supposed to start from a segment forming a transient β-structure. As the application to the monomeric tau protein of standard structural techniques, such as macromolecular crystallography or electron microscopy, is not possible, small-angle X-ray scattering provides a unique tool to obtain structural information on tau in solution and, more generally, on the whole IDP category [39][40][41][42][43][44][45][46].…”

Section: The Case Of Tau Proteinmentioning

confidence: 99%

“…SAXS measurements [44,45] have been acquired at the BioSAXS beamline ID 14-3 at ESRF (Grenoble, France) [46]. A pictorial view of the typical experimental geometry of a SAXS experiment is presented in Fig.…”

Section: Small-angle X-ray Scattering (Saxs) Measurementsmentioning

confidence: 99%

See 2 more Smart Citations

Temperature and solvent dependence of the dynamical landscape of tau protein conformations

et al. 2011

View full text Add to dashboard Cite

We report the variation with temperature of the ensemble distribution of conformations spanned by the tau protein in its dynamical states measured by small-angle X-ray scattering (SAXS) using synchrotron radiation. The SAXS data show a clear temperature variation of the distribution of occupied protein conformations from 293 to 318 K. More conformations with a smaller radius of gyration are occupied at higher temperature. The protein-solvent interactions are shown by computer simulation to be essential for controlling the dynamics of protein conformations, providing evidence for the key role of water solvent in the protein dynamics, as proposed by Giorgio Careri.Keywords Protein conformations · Intrinsic disordered proteins · Water effect in conformational landscape · Temperature effects in protein fluctuations

show abstract

Section: Saxs Resultsmentioning

confidence: 98%

Section: The Case Of Tau Proteinmentioning

confidence: 99%

See 1 more Smart Citation

Temperature and solvent dependence of the dynamical landscape of tau protein conformations

et al. 2011

View full text Add to dashboard Cite

show abstract

“…48,49 RSL bound to Mefuc or to Fuc-PEG was characterized at four different protein concentrations (10, 5, 2 and 1 mg/ml) using the automated sample changer. 50 Data were collected also on a sample of the conjugate that was pre-treated via an online SEC at BM29.…”

Section: Saxs Characterizationmentioning

confidence: 99%

Noncovalent PEGylation via Lectin–Glycopolymer Interactions

et al. 2016

View full text Add to dashboard Cite

The full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 2 AbstractPEGylation, the covalent modification of proteins with polyethylene glycol, is an abundantly used technique to improve the pharmacokinetics of therapeutic proteins. The drawback with this methodology is that the covalently attached PEG can impede the biological activity (e.g. reduced receptor-binding capacity). Protein therapeutics with "disposable" PEG modifiers have potential advantages over the current technology. Here, we show that a protein-polymer "Medusa complex" is formed by the combination of a hexavalent lectin with a glycopolymer. Using NMR spectroscopy, small angle X-ray scattering (SAXS), size exclusion chromatography and native gel electrophoresis it was demonstrated that the fucose-binding lectin RSL and a fucose-capped polyethylene glycol (Fuc-PEG) form a multimeric assembly. All of the experimental methods provided evidence of noncovalent PEGylation with a concomitant increase in molecular mass and hydrodynamic radius. The affinity of the protein-polymer complex was determined by ITCand competition experiments to be in the µM range, suggesting that such systems have potential biomedical applications.

show abstract

“…Synchrotron X-ray scattering data were collected at the beamline BM29 (ESRF, Grenoble) [32] using a robot sample changer [33]. The Table 1 Crystal parameters, data collection statistics and refinement statistics.…”

Section: Small Angle X-ray Scatteringmentioning

confidence: 99%

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Ilari

Alaleona

Tria

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

View full text Add to dashboard Cite

This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. Background: In Gram-negative bacteria the ZnuABC transporter ensures adequate zinc import in Zn(II)-poor environments, like those encountered by pathogens within the infected host. Recently, the metal-binding protein ZinT was suggested to operate as an accessory component of ZnuABC in periplasmic zinc recruitment. Since ZinT is known to form a ZinT-ZnuA complex in the presence of Zn(II) it was proposed to transfer Zn(II) to ZnuA. The present work was undertaken to test this claim. Methods: ZinT and its structural relationship with ZnuA have been characterized by multiple biophysical techniques (X-ray crystallography, SAXS, analytical ultracentrifugation, fluorescence spectroscopy). Results: The metal-free and metal-bound crystal structures of Salmonella enterica ZinT show one Zn(II) binding site and limited structural changes upon metal removal. Spectroscopic titrations with Zn(II) yield a K D value of 22 ± 2 nM for ZinT, while those with ZnuA point to one high affinity (K D b 20 nM) and one low affinity Zn(II) binding site (K D in the micromolar range). Sedimentation velocity experiments established that Zn(II)-bound ZinT interacts with ZnuA, whereas apo-ZinT does not. The model of the ZinT-ZnuA complex derived from small angle X-ray scattering experiments points to a disposition that favors metal transfer as the metal binding cavities of the two proteins face each other. Conclusions: ZinT acts as a Zn(II)-buffering protein that delivers Zn(II) to ZnuA. General significance: Knowledge of the ZinT-ZnuA relationship is crucial for understanding bacterial Zn(II) uptake.

show abstract

New beamline dedicated to solution scattering from biological macromolecules at the ESRF

Cited by 86 publications

References 3 publications

Temperature and solvent dependence of the dynamical landscape of tau protein conformations

Temperature and solvent dependence of the dynamical landscape of tau protein conformations

Noncovalent PEGylation via Lectin–Glycopolymer Interactions

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Contact Info

Product

Resources

About