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Diffraction quality crystals of protein-x from azotobacter-vinelandii

Academic Article
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Overview

authors

  • Diller, T. C.
  • Shaw, A.
  • Isas, J. M.
  • Burgess, B. K.
  • Stout, C. David

publication date

  • August 1994

journal

  • Journal of Molecular Biology  Journal

abstract

  • Protein X from Azotobacter vinelandii has recently been shown to be either a NADPH oxidase or a NADP+ reductase that interacts specifically with ferredoxin I. Single crystals have been obtained by vapor diffusion from polyethylene glycol 4000 solutions containing 100 mM citrate buffer (pH 5.5). The crystals belong to space group P2(1)2(1)2 with unit cell constants a = 68.9 A, b = 76.9 A, c = 52.8 A and one molecule (M(r) 29,000) per asymmetric unit. The crystals diffract to 2.5 A resolution.

subject areas

  • Azotobacter vinelandii
  • Bacterial Proteins
  • Crystallography, X-Ray
  • Ferredoxins
  • Oxidation-Reduction
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1994.1535

PubMed ID

  • 8057382
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Additional Document Info

start page

  • 620

end page

  • 621

volume

  • 241

issue

  • 4

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