Crystallization of mutant beta subunit of F1-ATPase from thermophilic Bacillus PS3

J Mol Biol. 1994 Oct 7;242(5):709-11. doi: 10.1006/jmbi.1994.1621.

Abstract

The mutant beta subunit of F1-ATPase from a thermophilic Bacillus strain, PS3, in which tyrosine at position 341 is replaced by leucine (beta Y341L) was expressed in Escherichia coli and crystallized by the vapor-diffusion procedure. Small needle-like crystals were obtained using ammonium sulfate as a precipitant and grown by the stepwise seeding method. The crystals obtained by this procedure diffracted X-rays to about 3 A resolution. The diffraction patterns indicated that the crystals belong to the orthorhombic system and the space group I222 or I2(1)2(1)2(1) with unit-cell dimensions of a = 232 A, b = 66 A, and c = 80 A. It is thought that the asymmetric unit comprises one beta Y341L molecule.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Proton-Translocating ATPases / chemistry*
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • Proton-Translocating ATPases