Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.
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.
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 108 Althouse Laboratory, University Park, PA 16802, USA.
B
B
Teo
R D
RD
Kidd
J
J
Mack
A
A
Tiwari
D
D
Hernandez
A T
AT
Phillips
G K
GK
Farber
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D006638:Histidine Ammonia-Lyase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D006638:Histidine Ammonia-Lyase