Expression, purification and preliminary diffraction studies of PhnP.
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 .
Podzelinska
Kateryna
K
Department of Biochemistry, Queen's University, Kingston K7L 3N6, Canada.
He
Shumei
S
Soares
Alexei
A
Zechel
David
D
Hove-Jensen
Bjarne
B
Jia
Zongchao
Z
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D063065:Organophosphonates / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction
D063065:Organophosphonates; D011994:Recombinant Proteins