2a5m
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2a5m.gif|left|200px]] | [[Image:2a5m.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2a5m", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2a5m| PDB=2a5m | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''NMR structure of murine gamma-S crystallin from joint refinement with SAXS data''' | '''NMR structure of murine gamma-S crystallin from joint refinement with SAXS data''' | ||
| Line 29: | Line 26: | ||
[[Category: Trewhella, J.]] | [[Category: Trewhella, J.]] | ||
[[Category: Wu, J.]] | [[Category: Wu, J.]] | ||
| - | [[Category: | + | [[Category: Alignment]] |
| - | [[Category: | + | [[Category: Deuteration]] |
| - | [[Category: | + | [[Category: Liquid crystal]] |
| - | [[Category: | + | [[Category: Mfr]] |
| - | [[Category: | + | [[Category: Molecular fragment replacement]] |
| - | [[Category: | + | [[Category: Pf1]] |
| - | [[Category: | + | [[Category: Rdc]] |
| - | [[Category: | + | [[Category: Residual dipolar coupling]] |
| - | [[Category: | + | [[Category: Sax]] |
| - | [[Category: | + | [[Category: Small-angle x-ray scattering]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:38:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:38, 3 May 2008
NMR structure of murine gamma-S crystallin from joint refinement with SAXS data
Overview
Determination of the 3D structures of multidomain proteins by solution NMR methods presents a number of unique challenges related to their larger molecular size and the usual scarcity of constraints at the interdomain interface, often resulting in a decrease in structural accuracy. In this respect, experimental information from small-angle scattering of X-ray radiation in solution (SAXS) presents a suitable complement to the NMR data, as it provides an independent constraint on the overall molecular shape. A computational procedure is described that allows incorporation of such SAXS data into the mainstream high-resolution macromolecular structure refinement. The method is illustrated for a two-domain 177-amino-acid protein, gammaS crystallin, using an experimental SAXS data set fitted at resolutions from approximately 200 A to approximately 30 A. Inclusion of these data during structure refinement decreases the backbone coordinate root-mean-square difference between the derived model and the high-resolution crystal structure of a 54% homologous gammaB crystallin from 1.96 +/- 0.07 A to 1.31 +/- 0.04 A. Combining SAXS data with NMR restraints can be accomplished at a moderate computational expense and is expected to become useful for multidomain proteins, multimeric assemblies, and tight macromolecular complexes.
About this Structure
2A5M is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data., Grishaev A, Wu J, Trewhella J, Bax A, J Am Chem Soc. 2005 Nov 30;127(47):16621-8. PMID:16305251 Page seeded by OCA on Sat May 3 18:38:22 2008
