Crystallization and preliminary X-ray analysis of the controller protein C.AhdI from Aeromonas hydrophilia

Authors: McGeehan, J. E.; Streeter, S.; Cooper, J. B.; Mohammed, F.; Fox, G. C.; Kneale, G. G.

Source: Acta Crystallographica Section D, Volume 60, Number 2, 1 February 2004 , pp. 323-325(3)

Publisher: Blackwell Publishing

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Abstract:

Single crystals of purified homodimeric controller protein from Aeromonas hydrophilia (C.AhdI) have been grown under several different conditions using vapour diffusion. X-ray diffraction data have been collected using synchrotron radiation from crystals of both the native and a selenomethionine (SeMet) derivative of the protein. The native crystal form belongs to space group P2₁ and data were collected to a resolution of 2.2 Å. Two crystal forms of the SeMet protein have been obtained and were found to belong to space groups P1 and P2₁; data have been recorded to 2.0 and 1.7 Å resolution, respectively, for the two crystal forms. Three-wavelength MAD data were collected to 1.7 Å for the SeMet derivative crystal, which is isomorphous with the native P2₁ crystal.

Keywords: Aeromonas hydrophilia; DNA-binding proteins; DNA-modification methylases

Document Type: Research article

DOI: 10.1107/S0907444903026143

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