2A5M
NMR structure of murine gamma-S crystallin from joint refinement with SAXS data
Summary for 2A5M
| Entry DOI | 10.2210/pdb2a5m/pdb |
| Related | 1A45 1A5D 1A7H 1AG4 1AMM 1HK0 1ZWM 1ZWO |
| Descriptor | Gamma crystallin S (1 entity in total) |
| Functional Keywords | saxs, small-angle x-ray scattering, alignment, deuteration, liquid crystal, pf1, rdc, residual dipolar coupling, molecular fragment replacement, mfr, structural protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20747.27 |
| Authors | Grishaev, A.,Wu, J.,Trewhella, J.,Bax, A. (deposition date: 2005-06-30, release date: 2005-07-19, Last modification date: 2024-05-22) |
| Primary citation | Grishaev, A.,Wu, J.,Trewhella, J.,Bax, A. Refinement of Multidomain Protein Structures by Combination of Solution Small-Angle X-ray Scattering and NMR Data. J.Am.Chem.Soc., 127:16621-16628, 2005 Cited by PubMed Abstract: 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. PubMed: 16305251DOI: 10.1021/ja054342m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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