Open AccessExpression, purification and preliminary diffraction studies of PhnP
Author(s) -
Podzelinska Kateryna,
He Shumei,
Soares Alexei,
Zechel David,
HoveJensen Bjarne,
Jia Zongchao
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108014656
Subject(s) - escherichia coli , operon , diffraction , phosphonate , crystallography , chemistry , bacteria , biochemistry , biology , gene , genetics , physics , optics
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 Å and the crystals belonged to space group C 2, with unit‐cell parameters a = 111.65, b = 75.41, c = 83.23 Å, α = γ = 90, β = 126.3°.