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Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the histone‐like HU protein from Spiroplasma melliferum KC3
Author(s) -
Boyko Konstantin,
Gorbacheva Marina,
Rakitina Tatiana,
Korzhenevskiy Dmitry,
Vanyushkina Anna,
Kamashev Dmitry,
Lipkin Alexey,
Popov Vladimir
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14025333
Subject(s) - crystallography , spiroplasma , nucleoid , escherichia coli , crystallization , resolution (logic) , microbiology and biotechnology , biology , histone , dna , monomer , chemistry , gene , nucleosome , mycoplasma , biochemistry , genetics , mollicutes , polymer , organic chemistry , artificial intelligence , computer science
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 C 2 and the structure of the protein was solved by the molecular‐replacement method with one monomer per asymmetric unit.