Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli.
ATP-phosphoribosyltransferase (ATP-PRT) from Escherichia coli has been purified and crystals were obtained by the vapour-diffusion method using sodium tartrate as a precipitant. Dynamic light scattering was used to assess conditions for the monodispersity of the enzyme. The crystals are trigonal, space group R32, with unit-cell parameters a = b = 133.6, c= 114.1 A (at 100 K), and diffract to 2.7 A on a synchrotron X-ray source. The asymmetric unit is likely to contain one molecule, corresponding to a packing density of 2.9 A3 Da(-1). A model for the quaternary structure is proposed based on the crystallographic symmetry.
Lohkamp
B
B
Division of Biochemistry and Molecular Biology, Institute of Biomedicaland Life Sciences, University of Glasgow, Glasgow, Scotland.
Coggins
J R
JR
Lapthorn
A J
AJ
D001276:ATP Phosphoribosyltransferase / Q000737:chemistry / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D008027:Light; D008958:Models, Molecular; D011487:Protein Conformation; D012542:Scattering, Radiation
D001276:ATP Phosphoribosyltransferase