PRELIMINARY CRYSTALLOGRAPHIC STUDY ON A LOW-MOLECULAR-WEIGHT FORM OF BACTERIAL PLASMINOGEN-ACTIVATOR STAPHYLOKINASE

Authors
CHATTOPADHYAY D STEWART JE SMITH CD DELUCAS LJ NARAYANA SVL
Citation
D. Chattopadhyay et al., PRELIMINARY CRYSTALLOGRAPHIC STUDY ON A LOW-MOLECULAR-WEIGHT FORM OF BACTERIAL PLASMINOGEN-ACTIVATOR STAPHYLOKINASE, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 480-481
Citations number
15
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
4
Pages
480 - 481
Database
ISI
SICI code
0907-4449(1997)53:<480:PCSOAL>2.0.ZU;2-D
Abstract
Staphylokinase, a 17 kDa protein, produced by certain strains of Staph ylococcus 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 residue s. This low molecular weight form of recombinant staphylokinase has be en crystallized using the hanging-drop vapor-diffusion technique with polyethylene glycol 4000 as precipitant. Crystals belong to the orthor hombic 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. T hese crystals diffract to about 2.4 Angstrom resolution.