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Fic domains in proteins are found in abundance in nature from the simplest prokaryotes to animals. Interestingly, Fic domains found in two virulence factors of Gram-negative bacteria have recently been demonstrated to catalyse the transfer of the AMP moiety from ATP to small host GTPases. This post-translational modification has attracted considerable interest and a role for adenylylation in pathology and physiology is emerging. This work was aimed at the structural characterization of a newly identified Fic protein of the Gram-positive bacterium Clostridium difficile. A constitutively active inhibitory helix mutant of C. difficile Fic was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion technique. Preliminary X-ray crystallo­graphic analysis shows that the crystals diffract to at least 1.68 Å resolution at a synchrotron X-ray source. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 45.6, b = 80.8, c = 144.7 Å, α = β = γ = 90°. Two molecules per asymmetric unit corresponds to a Matthews coefficient of 2.37 Å3 Da−1 and a solvent content of 48%.

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Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X1400987X/pg5042sup1.pdf
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