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Crystallization and preliminary X‐ray analysis of nonglycosylated tissue inhibitor of metalloproteinases‐1, N 30 QN 78 Q TIMP‐1
Author(s) -
Tolley Shirley P.,
Davies Gideon J.,
O'Shea Mark,
Cockett Mark I.,
Docherty Andrew J. P.,
Murphy Gillian
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340170410
Subject(s) - crystallization , resolution (logic) , crystallography , molecule , x ray , diffraction , x ray crystallography , matrix metalloproteinase , chemistry , stereochemistry , tartrate , biochemistry , optics , physics , organic chemistry , artificial intelligence , computer science
A nonglycosylated (N 30 QN 78 Q) form of the human tissue inhibitor of metalloproteinases, TIMP‐1, has been prepared and crystallized in a form suitable for X‐ray diffraction analysis. Small single crystals have been grown using sodium tartrate as a precipitant. The crystals are in space group P 2 1 , with cell dimensions a = 35.28, b = 53.95, c = 48.56, and β = 96.0°. There is a single molecule of TIMP‐1 in the asymmetric unit. The crystals diffract to at least 2.3 Å resolution. Complete data have been collected to 2.9 Å and a search for heavymetal derivatives is in progress. © 1993 Wiley‐Liss, Inc.