Crystallization and preliminary X-ray analysis of nonglycosylated tissue inhibitor of metalloproteinases-1, N30QN78Q TIMP-1.
A nonglycosylated (N30QN78Q) 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 P2(1), with cell dimensions a = 35.28, b = 53.95, c = 48.56, and beta = 96.0 degrees. There is a single molecule of TIMP-1 in the asymmetric unit. The crystals diffract to at least 2.3 A resolution. Complete data have been collected to 2.9 A and a search for heavy-metal derivatives is in progress.
Tolley
S P
SP
Department of Chemistry, University of York, Heslington, England.
Davies
G J
GJ
O'Shea
M
M
Cockett
M I
MI
Docherty
A J
AJ
Murphy
G
G
D001483:Base Sequence; D003461:Crystallography / Q000379:methods; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019714:Tissue Inhibitor of Metalloproteinases; D014961:X-Ray Diffraction / Q000379:methods
D006023:Glycoproteins; D019714:Tissue Inhibitor of Metalloproteinases; D008666:Metalloendopeptidases