Expression, Purification and Preliminary Diffraction Studies of PhnP

Journal Article · Mon Dec 31 23:00:00 EST 2007 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309108014656· OSTI ID:960087

Podzelinska, K; He, S; Soares, A; Zechel, D; Hove-Jensen, B; Jia, Z

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 Angstroms and the crystals belonged to space group C2, with unit-cell parameters a = 111.65, b = 75.41, c = 83.23 Angstroms, {alpha} = [gamma] = 90, {beta} = 126.3 .

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 960087
• Report Number(s): BNL--83073-2009-JA
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Vol. 64
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
BIOCHEMISTRY
CRYSTALS
DIFFRACTION
DIFFUSION
ESCHERICHIA COLI
PHOSPHONATES
PHOSPHORUS
PROTEINS
PURIFICATION
SPACE GROUPS
X-RAY DIFFRACTION
national synchrotron light source