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

Academic Article
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Overview

authors

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

publication date

  • 1999

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

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.

subject areas

  • Aldehyde-Lyases
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Recombinant Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444999006502

PubMed ID

  • 10393309
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Additional Document Info

start page

  • 1368

end page

  • 1369

volume

  • 55

issue

  • Pt 7

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