Crystallization and preliminary X-ray analysis of the Escherichia coli replication terminator protein complexed with DNA.
Crystals of the Escherichia coli replication terminator protein (Tus) complexed with its binding site DNA were obtained by a microdialysis method using PEG 4000. They belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with the unit cell parameter: a = 68.1 A, c = 230.7 A and contain one protein-DNA complex in an asymmetric unit. The native data set has been collected to 2.7 A resolution.
Kamada
K
K
Department of Genetics, Graduate University for Advanced Studies, Shizuoka, Japan.
Ohsumi
K
K
Horiuchi
T
T
Shimamoto
N
N
Morikawa
K
K
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D001483:Base Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; C062011:DNA replication terminus site-binding protein, E coli; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C061910:tus protein, Bacteria; C489236:tus protein, E coli; D004247:DNA