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

Okumura Mika | Zendy; Ishikawa Kohki | Zendy; Kanaya Shigenori | Zendy; Itaya Mitsuhiro | Zendy; Morikawa Kosuke | Zendy

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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.

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