Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.

@article{Teo1998CrystallizationAP,
  title={Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.},
  author={B Teo and Richard D. Kidd and John Mack and Arjun Tiwari and Damir Hernandez and Allen T. Phillips and Gregory K. Farber},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={1998},
  volume={54 Pt 4},
  pages={681-3}
}
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… CONTINUE READING