Structural studies of the Hrp secretion system: expression, purification, crystallization and preliminary X-ray analysis of the C-terminal domain of the HrcQB protein from Pseudomonas syringae pv. phaseolicola.
The C-terminal domain of the HrcQ(B) protein from the Hrp secretion system of the plant pathogenic bacterium Pseudomonas syringae pv. phaseolicola has been crystallized from MPD using the hanging-drop vapour-diffusion method. The crystals belong to space group P2(1), with unit-cell parameters a = 51.6, b = 27.3, c = 97.2 A and beta = 99.8 degrees. A complete native data set extending to 3.0 A resolution was collected from a single cryoprotected crystal. The crystal solvent content and calculation of self-rotation functions showing non-crystallographic twofold symmetry axes are consistent with the presence of an oligomeric assembly in the asymmetric unit.
Fadouloglou
V E
VE
University of Crete, Department of Biology, PO Box 2208, GR-71409 Heraklion, Crete, Greece.
Tampakaki
A P
AP
Panopoulos
N J
NJ
Kokkinidis
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000737:chemistry*
D001426:Bacterial Proteins; C441634:HrcQb protein, Pseudomonas syringae