Literature DB >> 8057366

The crystallization and preliminary X-ray analysis of allosteric chorismate mutase.

Y Xue1, W N Lipscomb.   

Abstract

An allosteric chorismate mutase, the Thr226-->Ile mutant, from the yeast Saccharomyces cerevisiae has been crystallized in space group P6(1)(P6(5)) using the hanging drop vapour diffusion method at room temperature. The cell dimensions are a = b = 95.8 A, c = 157.9 A, alpha = beta = 90 degrees, gamma = 120 degrees. It contains a dimer in the crystallographic asymmetric unit. The crystal diffracts to 2.2 A resolution. A native data set has been collected to 82% completeness at this resolution.

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Year:  1994        PMID: 8057366     DOI: 10.1006/jmbi.1994.1497

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.

Authors:  Sun Hur; Thomas C Bruice
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-29       Impact factor: 11.205

2.  The crystal structure of allosteric chorismate mutase at 2.2-A resolution.

Authors:  Y Xue; W N Lipscomb; R Graf; G Schnappauf; G Braus
Journal:  Proc Natl Acad Sci U S A       Date:  1994-11-08       Impact factor: 11.205

  2 in total

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