Expression, purification and preliminary diffraction studies of PhnP

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 -