Literature DB >> 15299920

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

D Chattopadhyay1, J E Stewart, C D Smith, L J DeLucas, S V Narayana.   

Abstract

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 A and one molecule in the asymmetric unit. These crystals diffract to about 2.4 A resolution.

Entities:  

Year:  1997        PMID: 15299920     DOI: 10.1107/S090744499700084X

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Enhanced protein fold recognition using secondary structure information from NMR.

Authors:  D J Ayers; P R Gooley; A Widmer-Cooper; A E Torda
Journal:  Protein Sci       Date:  1999-05       Impact factor: 6.725

  1 in total

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