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Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii.

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 P2(1), with unit-cell parameters a=54.4, b=53.8, c=82.6?Å, ?=106.1°. The crystals diffracted X-rays to 2.7?Å 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.

SUBMITTER: Oyenarte I

PROVIDER: S-EPMC3053155 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii.

Oyenarte Iker I Lucas María M Gómez García Inmaculada I Martínez-Cruz Luis Alfonso LA

Acta crystallographica. Section F, Structural biology and crystallization communications 20110223 Pt 3

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 P2(1), with unit-cell parameters a=54.4, b=53.8, c=82.6 Å, β=106.1°. The crystals diffracted X-rays to 2.7 Å resolution using synchrotron radiation. Matthews-volume calculations suggested the presence of two molecules in the asymmetric unit that are likel ...[more]

PMID: 21393835

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