Crystallization and preliminary X‐ray analysis of nonglycosylated tissue inhibitor of metalloproteinases‐1, N 30 QN 78 Q TIMP‐1 | Zendy

Tolley Shirley P. | Zendy; Davies Gideon J. | Zendy; O'Shea Mark | Zendy; Cockett Mark I. | Zendy; Docherty Andrew J. P. | Zendy; Murphy Gillian | Zendy

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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.

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