Crystallization And Preliminary X-Ray Crystallographic Studies Of Staphylokinase Variant S41g

Authors: Chen Y.; An J.; Song G.; Feng L.; Ding Y.; Chang Y.; Chen F.; Liu B.; He H.; Tang H.; Song H.; Rao Z.

Source: Protein and Peptide Letters, Volume 8, Number 6, December 2001 , pp. 503-507(5)

Publisher: Bentham Science Publishers

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Abstract:

Staphylokinse (Sak) is a plasminogen activator for the treatment of patients with thrombolitic disorders. However, the highly purified Sak can form dimer in solution, which is believed to be the cause for the increased antigenicity. Here we report a new crystal form with two molecules in an asymmetric unit, suggesting there maybe a dimer packing in crystal. The crystal belongs to the orthorhombic space group P2 1 2 1 2 1 and the unit cell dimensions are a=43.9, b=59.3, c=102.4 A, alpha=beta=gamma=90 degree. The diffraction data was 99.7percent complete to 2.3 A with an Rmerge of 5.5percent.

Keywords: Staphylokinse (Sak); plasminogen activator; thrombolitic disorders; Sak; SK streptokinase; Matrix assisted laser desorption; Staphylococcus aureus; plasminogen (Plg); plasmin (Pli)

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409148

Publication date: 2001-12-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.