Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 Å resolution from crystals grown following enzyme turnover

Abstract

Crystallization of Aspergillus nidulans 3-dehydroquinate synthase (DHQS), following turnover of the enzyme by addition of the substrate DAHP, gave ä new crystal form (form J). Although the crystals have dimensions of only 50 × 20 × 5 μm, they are well ordered, diffracting to 1.7 Å. The space group is C2221, with unit-cell parameters a = 90.0, b = 103.7, c = 177.4 Å. Structure determination and refinement to R = 0.19 (Rfree = 0.25) shows the DHQS is in the 'open' form with the substrate site unoccupied but with some loop regions perturbed. Previous crystals of open-form DHQS only diffracted to 2.5 Å resolution. The use of enzyme turnover may be applicable in other systems in attempts to improve crystal quality. © 2004 International Union of Crystallography. Printed in Denmark - all rights reserved.