Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian MSS4-Rab8 GTPase protein complex

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt 2):113-6. doi: 10.1107/S1744309105042995. Epub 2006 Jan 27.

Abstract

Rab GTPases function as ubiquitous key regulators of membrane-vesicle transport in eukaryotic cells. MSS4 is an evolutionarily conserved protein that binds to exocytotic Rabs and facilitates nucleotide release. The MSS4 protein in complex with nucleotide-free Rab8 GTPase has been purified and crystallized in a form suitable for structure analysis. The crystals belonged to space group P1, with unit-cell parameters a = 40.92, b = 49.85, c = 83.48 A, alpha = 102.88, beta = 97.46, gamma = 90.12 degrees. A complete data set has been collected to 2 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / isolation & purification*
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / isolation & purification*
  • Humans
  • Mice
  • rab GTP-Binding Proteins / chemistry
  • rab GTP-Binding Proteins / isolation & purification*

Substances

  • Guanine Nucleotide Exchange Factors
  • RABIF protein, human
  • GTP Phosphohydrolases
  • rab GTP-Binding Proteins