| Literature DB >> 16511013 |
Jill R Cupp-Vickery1, Robert Y Igarashi, Christopher R Meyer.
Abstract
ADP-glucose pyrophosphorylase catalyzes the conversion of glucose-1-phosphate and ATP to ADP-glucose and pyrophosphate, a key regulated step in both bacterial glycogen and plant starch biosynthesis. Crystals of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens (420 amino acids, 47 kDa) have been obtained by the sitting-drop vapor-diffusion method using lithium sulfate as a precipitant. A complete native X-ray diffraction data set was collected to a resolution of 2.0 A from a single crystal at 100 K. The crystals belong to space group I222, with unit-cell parameters a = 92.03, b = 141.251, c = 423.64 A. To solve the phase problem, a complete anomalous data set was collected from a selenomethionyl derivative. These crystals display one-fifth of the unit-cell volume of the wild-type crystals, with unit-cell parameters a = 85.38, b = 93.79, c = 140.29 A and space group I222.Entities:
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Year: 2005 PMID： 16511013 PMCID： PMC1952281 DOI： 10.1107/S1744309105002265
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091