Crystallization and preliminary X-ray crystallographic analysis of the N-terminal domain of XpsE protein from Xanthomonas campestris, an essential component of the type II protein-secretion machinery.
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. A 98.5% complete native data set from a frozen crystal has been collected to 2.0 A 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(3) Da(-1) and a solvent content of 36.1%.
Chen
Yeh
Y
Institute of Biochemistry, College of Life Sciences, National Chung Hsing University, Taichung City, Taiwan.
Hu
Nien Tai
NT
Chan
Nei Li
NL
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins; D016959:Xanthomonas campestris / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; C071567:general secretion pathway protein, Xanthomonas campestris