Literature DB >> 9757130

Crystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8.

T Nakai1, K Okada, S Kawaguchi, R Kato, S Kuramitsu, K Hirotsu.   

Abstract

Recombinant aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8, has been crystallized in two different crystal forms. The crystals of both forms are orthorhombic and belong to space group P212121 with cell dimensions a = 124.3, b = 113.6 and c = 61.6 A for form I and a = 197.3, b = 109.7 and c = 80.3 A for form II. The crystals of form I and II diffract to 2.1 and 2.5 A resolution, respectively, on a conventional laboratory rotating-anode source. Two heavy-atom derivatives have been identified for form I.

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Year:  1998        PMID: 9757130     DOI: 10.1107/s090744499800434x

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


  1 in total

1.  Molecular modeling and site-directed mutagenesis reveal essential residues for catalysis in a prokaryote-type aspartate aminotransferase.

Authors:  Fernando de la Torre; Aurelio A Moya-García; María-Fernanda Suárez; Carlos Rodríguez-Caso; Rafael A Cañas; Francisca Sánchez-Jiménez; Francisco M Cánovas
Journal:  Plant Physiol       Date:  2009-01-28       Impact factor: 8.340

  1 in total

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