Skip to Content
Merck
  • 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.

Acta crystallographica. Section F, Structural biology and crystallization communications (2007-11-17)
Mitsuhiro Nishimura, Tatsuya Kaminishi, Masahito Kawazoe, Mikako Shirouzu, Chie Takemoto, Shigeyuki Yokoyama, Akiko Tanaka, Sumio Sugano, Takuya Yoshida, Tadayasu Ohkubo, Yuji Kobayashi
PMID18007048
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.