Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis

  • Feifei Lu
  • , Feng Gao
  • , Honglin Li
  • , Weimin Gong
  • , Lin Zhou*
  • , Lijun Bi
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The conserved protein Rv3705c from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as a precipitant. The Rv3705c crystals exhibited space group P6122 or P6522, with unit-cell parameters a = b = 198.0, c = 364.1 Å, α = β = 90, γ = 120°, and diffracted to a resolution of 3.3 Å.

Original languageEnglish
Pages (from-to)1090-1092
Number of pages3
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number8
DOIs
StatePublished - Aug 2014
Externally publishedYes

Keywords

  • Mycobacterium tuberculosis
  • Rv3705c

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