Preliminary crystallographic study of Escherichia coli RuvC protein. An endonuclease specific for Holliday junctions.
Single crystals of the RuvC protein, an Escherichia coli endonuclease specific for Holliday junctions, were grown by the microdialysis method. The crystals belong to the space group P2(1), with unit cell dimensions a = 72.8 A, b = 139.6 A, c = 32.4 A and beta = 93.0 degrees, and contain four molecules in an asymmetric unit. Diffraction data to a Bragg spacing of 2.5 A resolution has been obtained using a synchrotron X-ray source.
Ariyoshi
M
M
Protein Engineering Research Institute, Osaka, Japan.
Vassylyev
D G
DG
Iwasaki
H
H
Fujishima
A
A
Shinagawa
H
H
Morikawa
K
K
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004260:DNA Repair / Q000235:genetics; D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D011995:Recombination, Genetic
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C069806:ruvC protein, E coli; D004706:Endodeoxyribonucleases