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Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli.

Authors :
Lapkouski, Mikalai
Panjikar, Santosh
Kuta Smatanova, Ivana
Csefalvay, Eva
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Jul2007, Vol. 63 Issue 7, p582-585. 4p. 2 Diagrams, 1 Chart, 1 Graph.
Publication Year :
2007

Abstract

EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I has been extensively characterized biochemically, there is no direct structural information available about particular subunits. HsdR is a motor subunit that is responsible for ATP hydrolysis, DNA translocation and cleavage of the DNA substrate recognized by the complex. Recombinant HsdR subunit was crystallized using the sitting-drop vapour-diffusion method. Crystals belong to the primitive monoclinic space group, with unit-cell parameters a = 85.75, b = 124.71, c = 128.37 Å, β = 108.14°. Native data were collected to 2.6 Å resolution at the X12 beamline of EMBL Hamburg. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
63
Issue :
7
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
25654028
Full Text :
https://doi.org/10.1107/S174430910702622X