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Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase
1Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 108 Althouse Laboratory, University Park, PA 16802, USA.
Abstract:
Histidine ammonium-lyase from P. putida was expressed in Escherichia coli, purified to homogeneity, and crystallized by the vapour-diffusion method using polyethylene glycol 3350 as the precipitant. The crystals, which diffract to at least 2.5 A resolution, exhibit the symmetry of space group P212121, with unit-cell parameters a = 89.7, b = 138.2 and c = 164.8 A. The asymmetric unit contains a tetramer, and the crystals have a Vm value of 2.41 A3 Da-1.

