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Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8
Author(s) -
Okumura Mika,
Ishikawa Kohki,
Kanaya Shigenori,
Itaya Mitsuhiro,
Morikawa Kosuke
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340150114
Subject(s) - thermus thermophilus , crystallization , crystallography , thermophile , hexagonal crystal system , molecule , chemistry , ribonuclease , biochemistry , enzyme , rna , organic chemistry , escherichia coli , gene
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 1 22 (or P6 5 22), 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.