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Crystallization and preliminary crystallographic studies of L30e, a ribosomal protein from Methanocaldococcus jannaschii (MJ1044).

ABSTRACT: In view of the biological significance of understanding the ribosomal machinery of both prokaryotes and eukaryotes, the L30e ribosomal protein from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized using the microbatch-under-oil method with the crystallization conditions 40% PEG 400, 0.1 M MES pH 6.0 and 5% PEG 3000 at 291 K. A diffraction-quality crystal (0.20 x 0.20 x 0.35 mm) was obtained that belonged to the primitive tetragonal space group P4(3), with unit-cell parameters a = 46.1, b = 46.1, c = 98.5 A, and diffracted to a resolution of 1.9 A. Preliminary calculations reveal that the asymmetric unit contains two monomers with a Matthews coefficient (V(M)) of 2.16 A(3) Da(-1).

SUBMITTER: Rangarajan S 

PROVIDER: S-EPMC2374168 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic studies of L30e, a ribosomal protein from Methanocaldococcus jannaschii (MJ1044).

Rangarajan Sarani S   Jeyakanthan Jeyaraman J   Mridula Palappetty P   Sakamoto Keiko K   Kitamura Yoshiaki Y   Agari Yoshihiro Y   Shinkai Akeo A   Ebihara Akio A   Kuramitsu Seiki S   Yokoyama Shigeyuki S   Sekar Kanagaraj K  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080131 Pt 2

In view of the biological significance of understanding the ribosomal machinery of both prokaryotes and eukaryotes, the L30e ribosomal protein from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized using the microbatch-under-oil method with the crystallization conditions 40% PEG 400, 0.1 M MES pH 6.0 and 5% PEG 3000 at 291 K. A diffraction-quality crystal (0.20 x 0.20 x 0.35 mm) was obtained that belonged to the primitive tetragonal space group P4(3), with unit-c  ...[more]

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