TY - JOUR
T1 - Expression, purification and preliminary diffraction studies of PhnP
AU - Podzelinska, Kateryna
AU - He, Shumei
AU - Soares, Alexei
AU - Zechel, David
AU - Hove-Jensen, Bjarne
AU - Jia, Zongchao
N1 - Keywords: Cloning, Molecular; Escherichia coli; Phosphonic Acids; Recombinant Proteins; X-Ray Diffraction
PY - 2008
Y1 - 2008
N2 - PhnP belongs to a 14-gene operon that supports the growth of Escherichia coli on alkylphosphonates as a sole source of phosphorus; however, the exact biochemistry of phosphonate degradation by this pathway is poorly understood. The protein was recombinantly expressed in Escherichia coli and purified to homogeneity. Sitting-drop vapour diffusion in combination with microseeding was used to obtain crystals that were suitable for X-ray diffraction. Data were collected to 1.3 A and the crystals belonged to space group C2, with unit-cell parameters a = 111.65, b = 75.41, c = 83.23 A, alpha = gamma = 90, beta = 126.3 degrees .
AB - PhnP belongs to a 14-gene operon that supports the growth of Escherichia coli on alkylphosphonates as a sole source of phosphorus; however, the exact biochemistry of phosphonate degradation by this pathway is poorly understood. The protein was recombinantly expressed in Escherichia coli and purified to homogeneity. Sitting-drop vapour diffusion in combination with microseeding was used to obtain crystals that were suitable for X-ray diffraction. Data were collected to 1.3 A and the crystals belonged to space group C2, with unit-cell parameters a = 111.65, b = 75.41, c = 83.23 A, alpha = gamma = 90, beta = 126.3 degrees .
U2 - 10.1107/S1744309108014656
DO - 10.1107/S1744309108014656
M3 - Journal article
C2 - 18540074
SN - 2053-230X
VL - 64
SP - 554
EP - 557
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - Pt 6
ER -