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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):950-2. doi: 10.1107/S1744309107048142. Epub 2007 Oct 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Humans
  • Ribosomal Protein L10
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / isolation & purification
  • Tumor Suppressor Proteins / chemistry*
  • Tumor Suppressor Proteins / isolation & purification

Substances

  • RPL10 protein, human
  • Ribosomal Proteins
  • Tumor Suppressor Proteins