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

M. Okumura, K. Ishikawa, S. Kanaya, Mitsuhiro Itaya, K. Morikawa

Research output: Contribution to journalArticle

1 Citation (Scopus)


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 P6122 (or P6522), 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.

Original languageEnglish
Pages (from-to)108-111
Number of pages4
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - 1993
Externally publishedYes



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

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

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