Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine
In this study, MtaN-1 from Aeromonas hydrophila was successfully expressed and purified using Ni–NTA affinity, Q anion-exchange and gel-filtration chromatography. Crystals of the protein in complex with the substrate SAH were obtained and diffracted to a resolution of 1.4 Å. The crystals belonged to the trigonal space group P3121 or P3221, with unit-cell parameters a = b = 102.7, c = 118.8 Å. The asymmetric unit contained two molecules of MtaN-1 complexed with SAH.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Xu, Y.Quan, C.-S.Jin, X.Jin, X.Zhao, J.Jin, L.Kim, J.-S.Guo, J.Fan, S.Ha, N.-C. Tags: Aeromonas hydrophila MtaN-1 S-adenosylmethionine research communications Source Type: research