Structural highlights
Publication Abstract from PubMed
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 degrees C. The crystals diffracted to 1.36 A 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.
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 Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):24-7. doi:, 10.1107/S2053230X14025333. Epub 2015 Jan 1. PMID:25615963[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyko K, Gorbacheva M, Rakitina T, Korzhenevskiy D, Vanyushkina A, Kamashev D, Lipkin A, Popov V. Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3. Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):24-7. doi:, 10.1107/S2053230X14025333. Epub 2015 Jan 1. PMID:25615963 doi:http://dx.doi.org/10.1107/S2053230X14025333
