In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 70, No. 4 ( 2014-04-01), p. 489-492
Abstract:
Independently of the restriction (HsdR) subunit, the specificity (HsdS) and methylation (HsdM) subunits interact with each other, and function as a methyltransferase in type I restriction–modification systems. A single gene that combines the HsdS and HsdM subunits in Vibrio vulnificus YJ016 was expressed and purified. A crystal suitable for X-ray diffraction was obtained from 25%( w / v ) polyethylene glycol monomethylether 5000, 0.1 M HEPES pH 8.0, 0.2 M ammonium sulfate at 291 K by hanging-drop vapour diffusion. Diffraction data were collected to a resolution of 2.31 Å using synchrotron radiation. The crystal belonged to the primitive monoclinic space group P 2 1 , with unit-cell parameters a = 93.25, b = 133.04, c = 121.49 Å, β = 109.7°. With four molecules in the asymmetric unit, the crystal volume per unit protein weight was 2.61 Å 3 Da −1 , corresponding to a solvent content of 53%.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X14004543
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2014
detail.hit.zdb_id:
2175956-X
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