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Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):588-91. doi: 10.1107/S1744309110011851. Epub 2010 Apr 30.

Abstract

AlgX is a periplasmic protein required for the production of the exopolysaccharide alginate in Pseudomonas sp. and Azotobacter vinelandii. AlgX has been overexpressed and purified and diffraction-quality crystals have been grown using iterative seeding and the hanging-drop vapor-diffusion method. The crystals grew as flat plates with unit-cell parameters a = 46.4, b = 120.6, c = 86.9 A, beta = 95.7 degrees . The crystals exhibited the symmetry of space group P2(1) and diffracted to a minimum d-spacing of 2.1 A. On the basis of the Matthews coefficient (V(M) = 2.25 A(3) Da(-1)), two molecules were estimated to be present in the asymmetric unit.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Pseudomonas aeruginosa / chemistry*

Substances

  • Bacterial Proteins