Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):784-6. doi: 10.1107/S1744309107038328. Epub 2007 Aug 31.

Abstract

A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 A. Native 2 diffracted to 2.9 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 A. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / isolation & purification
  • Peptide Fragments / chemistry
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / isolation & purification

Substances

  • Heat-Shock Proteins
  • Peptide Fragments
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • HsP104 protein, S cerevisiae
  • Adenosine Triphosphatases