Preliminary X-ray characterization and phasing of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus

Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1670-3. doi: 10.1107/s0907444903014094. Epub 2003 Aug 19.

Abstract

The N-terminal type II cohesin from the cellulosomal ScaB subunit of Acetivibrio cellulolyticus was crystallized in two different crystal systems: orthorhombic (space group P2(1)2(1)2(1)), with unit-cell parameters a = 37.455, b = 55.780, c = 87.912 A, and trigonal (space group P3(1)21), with unit-cell parameters a = 55.088, b = 55.088, c = 112.553 A. The two crystals diffracted to 1.2 and 1.9 A, respectively. A selenomethionine derivative was also crystallized and exhibited trigonal symmetry (space group P3(1)21), with unit-cell parameters a = 55.281, b = 55.281, c = 112.449 A and a diffraction limit of 1.97 A. Initial phasing of the trigonal crystals was successfully performed by the SIRAS method using Cu Kalpha radiation with the selenomethionine derivative as a heavy-atom derivative. The structure of the orthorhombic crystal form was solved by molecular replacement using the coordinates of the trigonal form.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacteria, Anaerobic / enzymology*
  • Bacterial Proteins / chemistry
  • Cell Cycle Proteins
  • Cellulosomes / chemistry*
  • Chromosomal Proteins, Non-Histone
  • Cohesins
  • Crystallization / methods
  • Crystallography, X-Ray / methods*
  • Fungal Proteins
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / isolation & purification
  • Protein Structure, Tertiary
  • Selenomethionine

Substances

  • Bacterial Proteins
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • Fungal Proteins
  • Nuclear Proteins
  • Selenomethionine