Purification, crystallization and preliminary X-ray diffraction study of human ribosomal protein L10 core domain.
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.
Nishimura
Mitsuhiro
M
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.
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
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D000080882:Ribosomal Protein L10; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D025521:Tumor Suppressor Proteins / Q000737:chemistry* / Q000302:isolation & purification
C000630686:RPL10 protein, human; D012269:Ribosomal Proteins; D025521:Tumor Suppressor Proteins