Secretion of pre-folded extracellular proteins across the outer membrane of Gram-negative bacteria is mainly assisted by the type II secretion machinery composed of 12±15 proteins. Here, the crystallization and preliminary analysis of one of the essential components of Xanthomonas campestris secretion machinery, the 21 kDa N-terminal domain of XpsE protein (XpsE N ), are reported. XpsE N has been crystallized at 277 K using PEG 400 as precipitant. These crystals belong to the tetragonal space group P4 1 2 1 2 (or P4 3 2 1 2), with unit-cell parameters a = b = 56.1, c = 102.7 A Ê . A 98.5% complete native data set from a frozen crystal has been collected to 2.0 A Ê resolution at 100 K with an overall R merge of 5.0%. The presence of one subunit of XpsE N per asymmetric unit gives a crystal volume per protein weight (V M ) of 1.92 A Ê 3 Da À1 and a solvent content of 36.1%.
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