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Science 27 February 1987:
Vol. 235. no. 4792, pp. 1049 - 1053
DOI: 10.1126/science.235.4792.1049
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Articles

Solution of a Protein Crystal Structure with a Model Obtained from NMR Interproton Distance Restraints

AXEL T. BRÜNGER 1, ROBERT L. CAMPBELL 2, G. MARIUS CLORE 3, ANGELA M. GRONENBORN 3, MARTIN KARPLUS 1, GREGORY A. PETSKO 2, and MARTHA M. TEETER 4

1 Department of Chemistry, Harvard University, Cambridge, MA 02138.
2 Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
3 Max-Planck-Institut für Biochemie, D-8033 Martinsried bei München, Federal Republic of Germany.
4 Department of Chemistry, Boston College, Chestnut Hill, MA 02167.

Model calculations were performed to test the possibility of solving crystal structures of proteins by Patterson search techniques with three-dimensional structures obtained from nuclear magnetic resonance (NMR) interproton distance restraints. Structures for crambin obtained from simulated NMR data were used as the test system; the root-mean-square deviations of the NMR structures from the x-ray structure were 1.5 to 2.2 Å for backbone atoms and 2.0 to 2.8 Å for side-chain atoms. Patterson searches were made to determine the orientation and position of the NMR structures in the unit cell. The correct solution was obtained by comparing the rotation function results of several of the NMR structures and the average structure derived from them. Conventional refinement techniques reduced the R factor from 0.43 at 4 Å resolution to 0.27 at 2 Å resolution without inclusion of water molecules. The partially refined structure has root-mean-square backbone and side-chain atom deviations from the x-ray structure of 0.5 and 1.3 Å, respectively.

Submitted on August 13, 1986
Accepted on December 29, 1986


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement.
B Shaanan, A. Gronenborn, G. Cohen, G. Gilliland, B Veerapandian, D. Davies, and G. Clore (1992)
Science 257, 961-964
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Molecular Dynamics: Applications to Proteins.
M. Karplus, A.T. Brunger, R. Elber, and J. Kuriyan (1987)
Cold Spring Harb Symp Quant Biol 52, 381-390
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