Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.

ABSTRACT: 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

SUBMITTER: Rinaldelli M 

PROVIDER: S-EPMC4306559 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature