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

Boyko K; Gorbacheva M; Rakitina T; Korzhenevskiy D; Vanyushkina A; Kamashev D; Lipkin A; Popov V

doi:10.1107/S2053230X14025333

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

Boyko K ¹ , Gorbacheva M ¹ , Rakitina T ² , Korzhenevskiy D ² , Vanyushkina A ³ , Kamashev D ³ Show all authors , Lipkin A ² , Popov V ¹

Affiliations

¹ Laboratory of Enzyme Engineering, A. N. Bach Institute of Biochemistry, RAS, Leninsky Prospekt 33/2, Moscow 119071, Russian Federation
² The Protein Factory, NBICS Center, National Research Centre `Kurchatov Institute', Akad. Kurchatova Square 1, Moscow 123182, Russian Federation
³ SRI of Physical-Chemical Medicine, Malaya Pirogovskaya 1a, Moscow 119435, Russian Federation

Acta Crystallogr F Struct Biol Commun, 2015 Jan 01;71(Pt 1):24-7.

PMID: 25615963 DOI: 10.1107/S2053230X14025333

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 1.36 Å 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.

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