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Updated: Jul 16, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Crystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of
Jorge Andrade1, Amin Karmali, Maria A Carrondo
1Instituto de Tecnologia Química e Biológica, Universidade Técnica de Lisboa, Apartado 127, 2781-901 Oeiras, Portugal.
Abstract:
The aliphatic amidase (acylamide amidohydrolase; EC 3.5.1.4) from Pseudomonas aeruginosa is a hexameric enzyme composed of six identical subunits with a molecular weight of approximately 38 kDa. Since microbial amidases are very important enzymes in industrial biocatalysis, the structural characterization of this enzyme will help in the design of novel catalytic activities of commercial interest. The present study reports the successful crystallization of the wild-type amidase from P. aeruginosa. Native crystals were obtained and a complete data set was collected at 1.4 A resolution, although the crystals showed diffraction to 1.25 A resolution. The crystals were found to belong to space group P6(3)22, with unit-cell parameters a = b = 102.60, c = 151.71 A, and contain one molecule in the asymmetric unit.

