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Updated: Aug 11, 2026
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia
Nandini Sharma1, Jeffrey H Toney, Paula M D Fitzgerald
1Department of Medicinal Chemistry, Merck Research Laboratories, PO Box 2000, RY 50-105, Rahway, NJ 07065-0900, USA. nandini_sharma@merck.com
Abstract:
The CphA metallo-beta-lactamase from Aeromonas hydrophilia has been expressed, purified and crystallized by the hanging-drop vapor-diffusion method using ammonium sulfate as the precipitant. The crystals exhibit orthorhombic symmetry (P2(1)2(1)2), with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 A. There is one monomer in the asymmetric unit and the solvent content is estimated to be 44% by volume. A data set extending to 1.8 A has been measured.
