Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus

Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):758-60. doi: 10.1107/s0907444900004388.

Abstract

The matrix protein from Ebola virus is a membrane-associated molecule that plays a role in viral budding. Despite its functional similarity to other viral matrix proteins, it displays no sequence similarity and hence may have a distinct fold. X-ray diffraction quality crystals of the Ebola VP40 matrix protein were grown by the hanging-drop vapour-diffusion method. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 64.4, b = 91.1, c = 47.9 A, beta = 96.3 degrees. A data set to 1.9 A resolution has been collected using synchrotron radiation. The unit cell contains one molecule of molecular weight 35 kDa per asymmetric unit, with a corresponding volume solvent content of 35%.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Ebolavirus / chemistry*
  • Factor Xa / genetics
  • Genetic Vectors
  • Peptide Fragments / biosynthesis
  • Peptide Fragments / genetics
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Viral Matrix Proteins / biosynthesis
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / genetics
  • Viral Matrix Proteins / isolation & purification
  • Viral Proteins / biosynthesis
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / isolation & purification

Substances

  • Peptide Fragments
  • Recombinant Fusion Proteins
  • VP40 protein, virus
  • Viral Matrix Proteins
  • Viral Proteins
  • Factor Xa