Crystallization and preliminary X-ray analysis of TBP-interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis strain KOD1

Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):372-4. doi: 10.1107/s090744490202142x. Epub 2003 Jan 23.

Abstract

The 26 kDa TBP (TATA-binding protein) interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (Tk-TIP26) is a possible transcriptional regulatory protein in Thermococcales. Here, the crystallization of both the native and selenomethionine-substituted proteins and data collection are described. The native crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 73.83, c = 86.41 A, and diffract to 2.2 A using synchrotron radiation. MAD data was collected and a Bijvoet difference Patterson map showed strong peaks sufficient to determine the positions of the Se atoms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / biosynthesis
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray / methods
  • Escherichia coli / genetics
  • Selenomethionine / chemistry
  • Synchrotrons
  • TATA-Box Binding Protein / biosynthesis
  • TATA-Box Binding Protein / chemistry*
  • TATA-Box Binding Protein / genetics
  • Thermococcus / chemistry*
  • Thermococcus / genetics

Substances

  • Archaeal Proteins
  • TATA-Box Binding Protein
  • Selenomethionine