Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8.
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 A, c = 314.7 A. They contain one 18,000 Mr molecule per asymmetric unit and diffract to 2.8 A resolution.
Okumura
M
M
Protein Engineering Research Institute, Osaka, Japan.
Ishikawa
K
K
Kanaya
S
S
Itaya
M
M
Morikawa
K
K
D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D016914:Ribonuclease H / Q000737:chemistry* / Q000235:genetics; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D016914:Ribonuclease H