Literature DB >> 8819175

Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus.

M Moser1, R Müller, N Battchikova, M Koivulehto, T Korpela, J N Jansonius.   

Abstract

Recombinant phosphoserine aminotransferase (EC 2.6.1.52) from Bacillus circulans subsp. alkalophilus was crystallized at room temperature from 0.1 M sodium acetate buffer, pH 4.6, and 2% PEG 20000, using macroseeding techniques. The crystals diffract X-rays to at least 2.0 A nominal resolution. They belong to space group C2 with unit cell dimensions a = 93.2 A, b = 93.1 A, c = 45.6 A, alpha = 90.0 degrees, beta = 106.8 degrees, gamma = 90.0 degrees. A native data set to 2.3 A has been collected. Assuming an average packing density of the crystals, there is one monomer in the asymmetric unit, resulting in a calculated solvent content of 48.2%.

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Year:  1996        PMID： 8819175      PMCID： PMC2143461          DOI： 10.1002/pro.5560050721

Source DB:  PubMed          Journal:  Protein Sci        ISSN： 0961-8368            Impact factor:   6.725


  8 in total

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6.  Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure.

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7.  Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase.

Authors:  M D Toney; E Hohenester; J W Keller; J N Jansonius
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8.  Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.

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  8 in total
  1 in total

1.  Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.

Authors:  Anatoly P Dubnovitsky; Evangelia G Kapetaniou; Anastassios C Papageorgiou
Journal:  Protein Sci       Date:  2005-01       Impact factor: 6.725
  1 in total

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