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

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

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

Mitsuhiro Nishimura,Tatsuya Kaminishi,Masahito Kawazoe,Mikako Shirouzu,Chie Takemoto,Shigeyuki Yokoyama,Akiko Tanaka,Sumio Sugano,Takuya Yoshida,Tadayasu Ohkubo,Yuji Kobayashi,Mitsuhiro Nishimura,Tatsuya Kaminishi,Masahito Kawazoe,Mikako Shirouzu,Chie Takemoto,Shigeyuki Yokoyama,Akiko Tanaka,Sumio Sugano,Takuya Yoshida,Tadayasu Ohkubo,Yuji Kobayashi,

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.

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

M Nishimura,T Kaminishi,M Kawazoe,M Shirouzu,C Takemoto,S Yokoyama,A Tanaka,S Sugano,T Yoshida,T Ohkubo,Y Kobayashi,M Nishimura,T Kaminishi,M Kawazoe,M Shirouzu,C Takemoto,S Yokoyama,A Tanaka,S Sugano,T Yoshida,T Ohkubo,Y Kobayashi,

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Acta crystallographica. Section F, Structural biol

VOLUME: 63

Page Numbers: 950-2

Journal Abbreviation: Acta Crystallogr. Sect. F Stru

ISSN: 1744-3091

DAY: 24

MONTH: 10

YEAR: 2007

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

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LANGUAGE: eng

NlmUniqueID: 101226117

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

AFFILIATION: Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.

Country: England

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MEDLINETA: Acta Crystallogr Sect F Struct

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