Preliminary crystallographic study on a low molecular weight form of bacterial plasminogen activator staphylokinase

被引：1

作者：

Chattopadhyay, D ^{[1
]}

Stewart, JE ^{[1
]}

Smith, CD ^{[1
]}

DeLucas, LJ ^{[1
]}

Narayana, SVL ^{[1
]}

机构：

[1] UNIV ALABAMA,SCH OPTOMETRY,BIRMINGHAM,AL 35294

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1997年 / 53卷

关键词：

D O I：

10.1107/S090744499700084X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Staphylokinase, a 17 kDa protein, produced by certain strains of Staphylococcus aureus functions as a fibrin-specific plasminogen activator. During its interaction with plasminogen, staphylokinase is converted into a low molecular weight form by loss of ten amino-terminal residues. This low molecular weight form of recombinant staphylokinase has been crystallized using the hanging-drop vapor-diffusion technique with polyethylene glycol 4000 as precipitant. Crystals belong to the orthorhombic space group C222(1) with unit-cell dimensions a = 43.78, b = 59.86 and c = 103.25 Angstrom and one molecule in the asymmetric unit. These crystals diffract to about 2.4 Angstrom resolution.

引用

页码：480 / 481

页数：2

共 15 条

[1] CLONING AND EXPRESSION IN ESCHERICHIA-COLI, BACILLUS-SUBTILIS, AND STREPTOCOCCUS-SANGUIS OF A GENE FOR STAPHYLOKINASE - A BACTERIAL PLASMINOGEN-ACTIVATOR [J].