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

Rangarajan, Sarani and Jeyakanthan, Jeyaraman and Palappetty, Mridula and Sakamoto, Keiko and Kitamura, Yoshiaki and Agari, Yoshihiro and Shinkai, Akeo and Ebihara, Akio and Kuramitsu, Seiki and Yokoyama, Shigeyuki and Sekar, Kanagaraj (2008) Crystallization and preliminary crystallographic studies of L30e, a ribosomal protein from Methanocaldococcus jannaschii (MJ1044). In: Acta Crystallographica Section F Structural Biology and Crystallization Communications, 64 . pp. 102-104.

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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 × 0.20 × 0.35 mm) was obtained that belonged to the primitive tetragonal space group P43, with unit-cell parameters a = 46.1, b = 46.1, c = 98.5 \AA, and diffracted to a resolution of 1.9 \AA. Preliminary calculations reveal that the asymmetric unit contains two monomers with a Matthews coefficient $(V_M)$ of 2.16 $\AA^3 Da^{-1}$.

Item Type:	Journal Article
Publication:	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher:	International Union of Crystallography
Additional Information:	Copyright of this article belongs to International Union of Crystallography.
Keywords:	ribosomal machinery; thermostability.
Department/Centre:	Division of Interdisciplinary Sciences > Supercomputer Education & Research Centre Division of Information Sciences (Doesn't exist now) > BioInformatics Centre
Date Deposited:	08 Mar 2008
Last Modified:	19 Sep 2010 04:43
URI:	http://eprints.iisc.ac.in/id/eprint/13358

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