Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction (Q27620941)

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G Moolenaar

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R Visse

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N Goosen

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X Vernede

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J C Fontecilla-Camps

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J Champness

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M R Sanderson

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901690-7

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language of work or name

English

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publication date

14 January 2000

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published in

FEBS Letters

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volume

465

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issue

2-3

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page(s)

161-4

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The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision

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Preparation of selenomethionyl proteins for phase determination

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Processing of X-ray diffraction data collected in oscillation mode

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Automated MAD and MIR structure solution

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[31] Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus

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Characterization of the Escherichia coli damage-independent UvrBC endonuclease activity

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Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC-DNA complex and in 3'-incision

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NMR assignments and secondary structure of the UvrC binding domain of UvrB

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Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement

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https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901690-7