Literature DB >> 10393309

Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli.

N C Blackwell1, P M Cullis, R A Cooper, T Izard.   

Abstract

2-Dehydro-3-deoxygalactarate (DDG) aldolase (E.C. 4.1.2.20) catalyzes the reversible aldol cleavage of DDG and 2-dehydro-3-deoxyglucarate to pyruvate and tartronic semialdehyde. Rhombohedral crystals of recombinant DDG aldolase from Escherichia coli K-12 were obtained. The crystals belong to space group R32 with unit-cell parameters a = 93 A, alpha = 85 degrees. The crystals diffract to beyond 1.8 A resolution on a Cu Kalpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 1.34 A3 Da-1.

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Year:  1999        PMID: 10393309     DOI: 10.1107/s0907444999006502

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


  2 in total

1.  Purification, crystallization and preliminary crystallographic studies on 2-dehydro-3-deoxygalactarate aldolase from Leptospira interrogans.

Authors:  Xu Li; Hua Huang; Xiaomin Song; Yanli Wang; Hang Xu; Maikun Teng; Weimin Gong
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-11-30

2.  Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.

Authors:  T Izard; N C Blackwell
Journal:  EMBO J       Date:  2000-08-01       Impact factor: 11.598

  2 in total

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