Open AccessPreliminary crystallographic analysis of ADP‐glucose pyrophosphorylase from Agrobacterium tumefaciens
Author(s) -
CuppVickery Jill R.,
Igarashi Robert Y.,
Meyer Christopher R.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002265
Subject(s) - agrobacterium tumefaciens , crystallography , chemistry , materials science , biochemistry , stereochemistry , transformation (genetics) , gene
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 Å from a single crystal at 100 K. The crystals belong to space group I 222, with unit‐cell parameters a = 92.03, b = 141.251, c = 423.64 Å. 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 Å and space group I 222.