PMID:11807275: Difference between revisions

Revision as of 18:08, 1 September 2013

Citation	No author listed (2002) Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:352-4
Abstract	Aspartokinase III catalyzes the commitment step in the aspartate metabolism pathway, the phosphorylation of aspartic acid. The Escherichia coli enzyme has been crystallized in the presence of its natural substrate (aspartic acid) and Mg-ADP and diffraction data has been collected at a synchroton source. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 60.44, b = 190.31, c = 99.55 A, and data 99.3% complete to 2.7 A. Solving the structure of AK III will provide the first structure of an aspartokinase from any organism.
Links	PubMed
Keywords	Adenosine Diphosphate/chemistry; Adenosine Diphosphate/metabolism; Aspartate Kinase/chemistry; Aspartate Kinase/isolation & purification; Aspartate Kinase/metabolism; Aspartic Acid/chemistry; Aspartic Acid/metabolism; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Image Processing, Computer-Assisted; Magnesium/chemistry; Magnesium/metabolism; Protein Conformation; Software
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