Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt 1):61-6. doi: 10.1107/S1744309105041400. Epub 2005 Dec 16.

Abstract

RuvBL1, an evolutionary highly conserved protein related to the AAA+ family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 A and three molecules in the asymmetric unit.

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics*
  • Carrier Proteins / isolation & purification
  • Conserved Sequence
  • Crystallization
  • Crystallography, X-Ray
  • DNA Helicases / chemistry*
  • DNA Helicases / genetics*
  • DNA Helicases / isolation & purification
  • Evolution, Molecular
  • Humans
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Recombinant Proteins
  • RuvB protein, Bacteria
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • RUVBL1 protein, human