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Updated: Jul 13, 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 DING protein from
Sebastien Moniot1, Mikael Elias, Donghyo Kim
1Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, CNRS-Université Henri Poincaré, 54506 Vandoeuvre-lès-Nancy, France.
Abstract:
PfluDING is a phosphate-binding protein expressed in Pseudomonas fluorescens. This protein is clearly distinct from the bacterial ABC transporter soluble phosphate-binding protein PstS and is more homologous to eukaryotic DING proteins. Interestingly, bacterial DING proteins have only been detected in certain Pseudomonas species. Although DING proteins seem to be ubiquitous in eukaryotes, they are systematically absent from eukaryotic genomic databases and thus are still quite mysterious and poorly characterized. PfluDING displays mitogenic activity towards human cells and binds various ligands such as inorganic phosphate, pyrophosphate, nucleotide triphosphates and cotinine. Here, the crystallization of PfluDING is reported in a monoclinic space group (P2(1)), with typical unit-cell parameters a = 36.7, b = 123.7, c = 40.8 A, alpha = 90, beta = 116.7, gamma = 90 degrees. Preliminary crystallographic analysis reveals good diffraction quality for these crystals and a 1.43 A resolution data set has been collected.
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