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Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 fromMethanocaldococcus jannaschii
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:318-324
- Publication Year :
- 2011
- Publisher :
- International Union of Crystallography (IUCr), 2011.
-
Abstract
- The purification and preliminary crystallographic analysis of the archaeal CBS-domain protein MJ1004 from Methanocaldococcus jannaschii are described. The native protein was overexpressed, purified and crystallized in the monoclinic space group P21, with unit-cell parameters a = 54.4, b = 53.8, c = 82.6 A, β = 106.1°. The crystals diffracted X-rays to 2.7 A resolution using synchrotron radiation. Matthews-volume calculations suggested the presence of two molecules in the asymmetric unit that are likely to correspond to a dimeric species, which is also observed in solution.
- Subjects :
- Models, Molecular
Archaeal Proteins
Molecular Sequence Data
Biophysics
CBS domain
Crystallography, X-Ray
Biochemistry
law.invention
Protein structure
Methanococcales
Structural Biology
law
Genetics
Molecule
Crystallization
biology
Resolution (electron density)
Methanocaldococcus jannaschii
Condensed Matter Physics
biology.organism_classification
Protein Structure, Tertiary
Crystallography
Crystallization Communications
Monoclinic crystal system
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 67
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....7094a3322019796424d18d103a8d84cf
- Full Text :
- https://doi.org/10.1107/s1744309110053479