Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8

Mika Okumura, Kohki Ishikawa, Shigenori Kanaya, Mitsuhiro Itaya, Kosuke Morikawa

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Ribonuclease H from an extreme thermophile, Thermus thermophilus HB8, has been crystallized from solutions at low ionic strength. The crystals belong to the hexagonal space group P6 122 (or P6 522), with unit cell parameters a = b = 44.7 Å, c = 314.7 Å. They contain one 18,000 Mr molecule per asymmetric unit and diffract to 2.8 Å resolution. © 1993 Wiley‐Liss, Inc.

Original languageEnglish
Pages (from-to)108-111
Number of pages4
JournalProteins: Structure, Function, and Bioinformatics
Volume15
Issue number1
DOIs
Publication statusPublished - 1993 Jan

Keywords

  • DNA/RNA hybrid
  • Thermus thermophilus HB8
  • X‐ray crystallography
  • crystallization
  • ribonuclease H

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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