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Crystallization and preliminary X-ray analysis of theEscherichia coli replication terminator protein complexed with DNA

โœ Scribed by Kamada, Katsuhiko; Ohsumi, Katsufumi; Horiuchi, Takashi; Shimamoto, Nobuo; Morikawa, Kosuke


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
212 KB
Volume
24
Category
Article
ISSN
0887-3585

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โœฆ Synopsis


Crystals of the Escherichia coli replication terminator protein (Tus) com- plexed with its binding site DNA were obtained by a microdialysis method using PEG 4000. They belong to the tetragonal space group P4,2,2 or P4,2,2 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.


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The POU domain, representing an approximately 150 amino acid conserved region, serves as the DNA-recognition domain for a large number of eukaryotic transcription factors. Bipartite in nature, the POU domain is comprised of a N-terminal POU-specific domain connected by a linker of variable length to