Expression, crystallization and preliminary crystallographic analysis of PilZ XAC1133 from Xanthomonas axonopodis pv. citri

Proteins containing PilZ domains are widespread in Gram‐negative bacteria and have recently been shown to be involved in the control of biofilm formation, adherence, aggregation, virulence‐factor production and motility. Furthermore, some PilZ domains have recently been shown to bind the second messenger bis(3′→5′)cyclic diGMP. Here, the cloning, expression, purification and crystallization of PilZ XAC1133 , a protein consisting of a single PilZ domain from Xanthomonas axonopodis pv. citri, is reported. The closest PilZ XAC1133 homologues in Pseudomonas aeruginosa and Neisseria meningitidis control type IV pilus function. Recombinant PilZ XAC1133 containing selenomethionine was crystallized in space group P 6 1 . The unit‐cell parameters were a = 62.125, b  = 62.125, c = 83.543 Å. These crystals diffracted to 1.85 Å resolution and a MAD data set was collected at a synchrotron source. The calculated Matthews coefficient suggested the presence of two PilZ XAC1133 molecules in the asymmetric unit.