期刊
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷 70, 期 -, 页码 958-967出版社
WILEY-BLACKWELL
DOI: 10.1107/S1399004713034160
关键词
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资金
- Ente Cassa di Risparmio di Firenze, MIUR [PRIN 2009FAKHZT]
- European Commission [261863]
- We-NMR [261572]
- BioMedBridges [284209]
- Instruct
- EU ESFRI Instruct Core Centre CERM, Italy
- MRC [MC_UP_A025_1012]
- MRC [MC_UP_A025_1012] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1012] Funding Source: researchfish
The program REFMAC5 from CCP4 was modified to allow the simultaneous use of X-ray crystallographic data and paramagnetic NMR data (pseudocontact shifts and self-orientation residual dipolar couplings) and/or diamagnetic residual dipolar couplings. Incorporation of these long-range NMR restraints in REFMAC5 can reveal differences between solid-state and solution conformations of molecules or, in their absence, can be used together with X-ray crystallographic data for structural refinement. Since NMR and X-ray data are complementary, when a single structure is consistent with both sets of data and still maintains reasonably 'ideal' geometries, the reliability of the derived atomic model is expected to increase. The program was tested on five different proteins: the catalytic domain of matrix metalloproteinase 1, GB3, ubiquitin, free calmodulin and calmodulin complexed with a peptide. In some cases the joint refinement produced a single model consistent with both sets of observations, while in other cases it indicated, outside the experimental uncertainty, the presence of different protein conformations in solution and in the solid state.
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