Crystallization and preliminary X-ray diffraction analysis of Langat virus envelope protein domain III

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1049-51. doi: 10.1107/s0907444903004475. Epub 2003 May 23.

Abstract

The putative receptor-binding domain (domain III) of the flavivirus Langat envelope glycoprotein has been crystallized using the hanging-drop vapor-diffusion method at 277 K. Two distinct crystal morphologies were observed to grow under the same conditions. The crystal forms both belong to a trigonal space group, P3(1)21 or P3(2)21, with unit-cell parameters a = 80.93, c = 132.1 A and a = 104.8, c = 219.5 A for forms I and II, respectively. Complete data sets to 2.9 and 3.35 A, respectively, have been collected at 100 K with Cu Kalpha X-rays from a rotating-anode generator.

Publication types

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

MeSH terms

  • Chromatography, Gel
  • Crystallization
  • Encephalitis Viruses, Tick-Borne / chemistry*
  • Encephalitis Viruses, Tick-Borne / genetics
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism
  • Membranes, Artificial
  • Plasmids / chemistry
  • Protein Conformation
  • Viral Envelope Proteins / chemistry*
  • X-Ray Diffraction

Substances

  • Membranes, Artificial
  • Viral Envelope Proteins