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Purification, crystallization and preliminary X-ray diffraction study of human ribosomal protein L10 core domain.

ABSTRACT: Eukaryotic ribosomal protein L10 is an essential component of the large ribosomal subunit, which organizes the architecture of the aminoacyl-tRNA binding site. The human L10 protein is also called the QM protein and consists of 214 amino-acid residues. For crystallization, the L10 core domain (L10CD, Phe34-Glu182) was recombinantly expressed in Escherichia coli and purified to homogeneity. A hexagonal crystal of L10CD was obtained by the sitting-drop vapour-diffusion method. The L10CD crystal diffracted to 2.5 A resolution and belongs to space group P3(1)21 or P3(2)21.

SUBMITTER: Nishimura M 

PROVIDER: S-EPMC2339757 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction study of human ribosomal protein L10 core domain.

Nishimura Mitsuhiro M   Kaminishi Tatsuya T   Kawazoe Masahito M   Shirouzu Mikako M   Takemoto Chie C   Yokoyama Shigeyuki S   Tanaka Akiko A   Sugano Sumio S   Yoshida Takuya T   Ohkubo Tadayasu T   Kobayashi Yuji Y  

Acta crystallographica. Section F, Structural biology and crystallization communications 20071024 Pt 11

Eukaryotic ribosomal protein L10 is an essential component of the large ribosomal subunit, which organizes the architecture of the aminoacyl-tRNA binding site. The human L10 protein is also called the QM protein and consists of 214 amino-acid residues. For crystallization, the L10 core domain (L10CD, Phe34-Glu182) was recombinantly expressed in Escherichia coli and purified to homogeneity. A hexagonal crystal of L10CD was obtained by the sitting-drop vapour-diffusion method. The L10CD crystal di  ...[more]

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