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Updated: Aug 22, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Crystallization and X-ray diffraction analyses of the outer membrane pyochelin receptor FptA from Pseudomonas
David Cobessi1, Hervé Célia, Franc Pattus
1Département Récepteurs et Protéines Membranaires, UPR 9050 CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67412 Illkirch, France. cobessi@esbs.u-strasbg.fr
Abstract:
FptA, the pyochelin outer membrane receptor from Pseudomonas aeruginosa, is a siderophore receptor involved in iron uptake when the bacterium grows under iron limitation. Two crystal forms of the FptA-pyochelin complex were obtained under different crystallization conditions. They belong to space groups P1 and P2(1)2(1)2(1) and data sets were collected for both crystal forms. The triclinic crystals diffract to 3.2 A resolution and the orthorhombic crystals show a 1.9 A resolution limit. A data set at the peak of the iron K edge was also collected at 3.1 A resolution.

