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)

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 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
Volume15
Issue number1
DOIs
Publication statusPublished - 1993
Externally publishedYes

Fingerprint

Thermus thermophilus
Ribonuclease H
Crystallization
Ionic strength
Osmolar Concentration
Crystals
Molecules

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8. / Okumura, M.; Ishikawa, K.; Kanaya, S.; Itaya, Mitsuhiro; Morikawa, K.

In: Proteins: Structure, Function and Genetics, Vol. 15, No. 1, 1993, p. 108-111.

Research output: Contribution to journalArticle

Okumura, M. ; Ishikawa, K. ; Kanaya, S. ; Itaya, Mitsuhiro ; Morikawa, K. / Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8. In: Proteins: Structure, Function and Genetics. 1993 ; Vol. 15, No. 1. pp. 108-111.
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