Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3

Konstantin Boyko, Marina Gorbacheva, Tatiana Rakitina, Dmitry Korzhenevskiy, Anna Vanyushkina, Dmitry Kamashev, Alexey Lipkin, Vladimir Popov

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

HU proteins belong to the nucleoid-associated proteins (NAPs) that are involved in vital processes such as DNA compaction and reparation, gene transcription etc. No data are available on the structures of HU proteins from mycoplasmas. To this end, the HU protein from the parasitic mycoplasma Spiroplasma melliferum KC3 was cloned, overexpressed in Escherichia coli and purified to homogeneity. Prismatic crystals of the protein were obtained by the vapour-diffusion technique at 4°C. The crystals diffracted to 1.36Å resolution (the best resolution ever obtained for a HU protein). The diffraction data were indexed in space group C2 and the structure of the protein was solved by the molecular-replacement method with one monomer per asymmetric unit.

Original languageEnglish
Pages (from-to)24-27
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume71
DOIs
Publication statusPublished - 1 Jan 2015
Externally publishedYes

Keywords

  • DNA binding
  • HU protein
  • three-dimensional structure

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