Crystallization and preliminary X-ray diffraction analysis of homing endonuclease I-Tsp061I.
Two crystal forms, rhombohedral and hexagonal, of a homing endonuclease from Thermoproteus sp. IC-061 (I-Tsp0611) were obtained by the hanging-drop and sitting-drop method, respectively. The hexagonal crystals belong to space group P6(3)22, with unit-cell parameters a = b = 111.4, c = 97.6 A, and diffract to 3.2 A resolution on beamline BL44 at SPring-8 (Harima, Japan). The rhombohedral crystals belong to space group R32, with unit-cell parameters a = b = 95.4, c = 192.9 A, and diffract to 2.7 A resolution using a Cu Kalpha rotating-anode generator with an R-AXIS VII detector. The crystal asymmetric unit contained one protein molecule and the solvent contents of the two crystal forms were estimated to be 68.3 and 67.6% by volume, respectively.
Imagawa
Takahito
T
Institute for Health Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima 770-8514, Japan.
Nakayama
Hitoshi
H
Katunuma
Nobuhiko
N
Sakuraba
Haruhiko
H
Ohshima
Toshihisa
T
Itoh
Takashi
T
Sako
Yoshihiko
Y
Nomura
Norimichi
N
Tsuge
Hideaki
H
D003460:Crystallization; D003850:Deoxyribonuclease I / Q000737:chemistry*; D041542:Thermoproteus / Q000201:enzymology*; D014961:X-Ray Diffraction
D003850:Deoxyribonuclease I