Expression, crystallization and preliminary X-ray analysis of the Pyrococcus abyssi protein homologue of Saccharomyces cerevisiae Nip7p

Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1925-8. doi: 10.1107/S0907444904020219. Epub 2004 Sep 23.

Abstract

Saccharomyces cerevisiae Nip7p is a nucleolar protein required for accurate processing of the 27S precursor of the 25S and 5.8S ribosomal RNAs. Nip7p homologues are found in eukaryotes and archaea. The Pyrococcus abyssi homologue of Nip7p (PaNip7) was cloned, expressed in Escherichia coli and purified for crystallization. X-ray diffraction data were collected from native crystals and an iodide derivative using synchrotron radiation. PaNip7 native crystals diffract to 1.8 A and belong to space group C2, with unit-cell parameters a = 88.49, b = 90.28, c = 63.35 A, beta = 134.29 degrees. The PaNip7 structure was solved using the SIRAS method.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Escherichia coli / metabolism
  • Pyrococcus abyssi / metabolism*
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Software

Substances

  • NIP7 protein, S cerevisiae
  • Ribosomal Proteins
  • Saccharomyces cerevisiae Proteins