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

Authors :
M.A. Gorbacheva
A.V. Lipkin
K.M. Boyko
D.A. Korzhenevskiy
Dmitry Kamashev
Vladimir Popov
Anna Vanyushkina
Tatiana V. Rakitina
Source :
Acta crystallographica. Section F, Structural biology communications. 71(Pt 1)
Publication Year :
2014

Abstract

HU proteins belong to the nucleoid-associated proteins (NAPs) that are involved in vital processes such as DNA compaction and reparation, gene transcriptionetc.No data are available on the structures of HU proteins from mycoplasmas. To this end, the HU protein from the parasitic mycoplasmaSpiroplasma melliferumKC3 was cloned, overexpressed inEscherichia coliand purified to homogeneity. Prismatic crystals of the protein were obtained by the vapour-diffusion technique at 4°C. The crystals diffracted to 1.36 Å resolution (the best resolution ever obtained for a HU protein). The diffraction data were indexed in space groupC2 and the structure of the protein was solved by the molecular-replacement method with one monomer per asymmetric unit.

Details

ISSN :
2053230X
Volume :
71
Issue :
Pt 1
Database :
OpenAIRE
Journal :
Acta crystallographica. Section F, Structural biology communications
Accession number :
edsair.doi.dedup.....95acc123ddc4d99799dbb19f639a70e3