Combining experimental information from crystal and solution studies: Joint x-ray and NMR refinement

Boaz Shaanan, Angela M. Gronenborn, Gerson H. Cohen, Gary L. Gilliland, B. Veerapandian, David R. Davies, G. Marius Clore

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Joint refinement of macromolecules against crystallographic and nuclear magnetic resonance (NMR) observations is presented as a way of combining experimental information from the two methods. The model of interleukin-1β derived by the joint x-ray and NMR refinement is shown to be consistent with the experimental observations of both methods and to have crystallographic R value and geometrical parameters that are of the same quality as or better than those of models obtained by conventional crystallographic studies. The few NMR observations that are violated by the model serve as an indicator for genuine differences between the crystal and solution structures. The joint x-ray-NMR refinement can resolve structural ambiguities encountered in studies of multidomain proteins, in which low- to medium-resolution diffraction data can be complemented by higher resolution NMR data obtained for the individual domains.

Original languageEnglish
Pages (from-to)961-964
Number of pages4
JournalScience
Volume257
Issue number5072
DOIs
StatePublished - 1 Jan 1992
Externally publishedYes

ASJC Scopus subject areas

  • General

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