PMID:11807275: Difference between revisions

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<span style = 'font-size: large'> '''Blanco, J and Viola, RE'''  (2002) Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.''Acta Crystallogr. D Biol. Crystallogr.'' '''58''':352-4</span>
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!align=left  |Citation
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'''Blanco, J and Viola, RE'''  (2002) Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli. ''Acta Crystallogr. D Biol. Crystallogr.'' '''58''':352-4
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!align=left  |Abstract
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11807275 PubMed]


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|{{TableHeadingColor}} |'''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.
!align=left  |Keywords
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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
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11807275 PubMed]
 
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Latest revision as of 04:16, 15 September 2013

Citation

Blanco, J and Viola, RE (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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