PMID:11185885
| Citation |
Lohkamp, B, Coggins, JR and Lapthorn, AJ (2000) Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:1488-91 |
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| Abstract |
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. |
| Links | |
| Keywords |
ATP Phosphoribosyltransferase/chemistry; ATP Phosphoribosyltransferase/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Light; Models, Molecular; Protein Conformation; Scattering, Radiation |
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