Crystals of ribosomal protein L1 from a hyperthermophilic archaeon Methanococcus jannaschii

Biochem Mol Biol Int. 1998 Jun;45(2):349-54. doi: 10.1080/15216549800202722.

Abstract

Crystallographic studies of ribosomal proteins from bacteria progressed rapidly during the last decade, though the structures of ribosomal proteins from other kingdoms have not yet been published. Here we describe crystals of archaeal ribosomal protein L1 from Methanococcus jannaschii. The protein crystals were grown in 10% PEG 10 K, 50 mM Hepes-HCl (pH 7.5) in hanging drops equilibrated against 33% PEG 10 K, 100 mM Hepes-HCl (pH 7.5). The crystals diffract to at least 2.5 A resolution and belong to the space group P1 with cell parameters a = 34.09 A, b = 39.39 A, c = 55.84 A, alpha = 83.65 degrees, beta = 80.38 degrees, gamma = 75.37 degrees.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Crystallography, X-Ray
  • Methanococcus / chemistry*
  • Recombinant Proteins / chemistry
  • Ribosomal Proteins / chemistry*

Substances

  • Archaeal Proteins
  • Recombinant Proteins
  • Ribosomal Proteins
  • ribosomal protein L1