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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3
- 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.
- Subjects :
- Spiroplasma
HU Protein
Spiroplasma melliferum
Biophysics
medicine.disease_cause
Crystallography, X-Ray
Biochemistry
Chromatography, Affinity
law.invention
Research Communications
Histones
chemistry.chemical_compound
Bacterial Proteins
Structural Biology
law
Genetics
medicine
Escherichia coli
Crystallization
biology
Protein Stability
Resolution (electron density)
X-ray
Condensed Matter Physics
Molecular biology
DNA-Binding Proteins
Crystallography
Histone
Monomer
chemistry
biology.protein
Subjects
Details
- ISSN :
- 2053230X
- Volume :
- 71
- Issue :
- Pt 1
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Accession number :
- edsair.doi.dedup.....95acc123ddc4d99799dbb19f639a70e3