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

Mark White, Deqian Liu, Michael R. Holbrook, Robert E. Shope, Alan Barrett, Robert O. Fox

Research output: Contribution to journalArticle

9 Citations (Scopus)

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, P3121 or P3221, with unit-cell parameters a = 80.93, c = 132.1 Å and a = 104.8, c = 219.5 Å for forms I and II, respectively. Complete data sets to 2.9 and 3.35 Å, respectively, have been collected at 100 K with Cu Kα X-rays from a rotating-anode generator.

Original languageEnglish (US)
Pages (from-to)1049-1051
Number of pages3
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number6
DOIs
StatePublished - Jun 1 2003

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Viral Envelope Proteins
Tick-Borne Encephalitis Viruses
Flavivirus
viruses
Crystallization
X-Ray Diffraction
X ray diffraction analysis
Glycoproteins
Electrodes
envelopes
X-Rays
crystallization
proteins
Crystals
crystal morphology
diffraction
Anodes
anodes
x rays
generators

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Crystallization and preliminary X-ray diffraction analysis of langat virus envelope protein domain III. / White, Mark; Liu, Deqian; Holbrook, Michael R.; Shope, Robert E.; Barrett, Alan; Fox, Robert O.

In: Acta Crystallographica - Section D Biological Crystallography, Vol. 59, No. 6, 01.06.2003, p. 1049-1051.

Research output: Contribution to journalArticle

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