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Protein Science, Vol 6, Issue 4 913-915, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals

T. IZARD, S. SARFATY, A. WESTPHAL, A. DE-KOK and WGJ. HOL
Howard Hughes Medical Institute, Biomolecular Structure Center and Departments of Biological Structure and Biochemistry, University of Washington, Seattle, Washington 98195-7742 Present address: Department of Biochemistry, University of Leicester, University Road, Leicester LE17RH, UK.

Members of the family of 2-oxoacid dehydrogenase multienzyme complexes catalyze the oxidative decarboxylation of {alpha}-keto acids and are among the most remarkable enzymatic machineries in the living cell. These multienzyme complexes combine a highly symmetric (cubic or icosahedral) core with a dynamic and flexible arrangement of numerous subunits and domains surrounding the core. The center of the complex is formed by either 24 or 60 copies of dihydrolipoamide acetyltransferase (E2)--a multidomain enzyme. The hollow icosahedral cores are composed of 60 identical subunits of the catalytic domain of E2 with a molecular weight of about 1.8 million Da. Bipyramidal crystals suitable for X-ray diffraction of the icosahedral core of the pyruvate dehydrogenase multienzyme complex from Enterococcus faecalis were grown up to 0.7 mm in each dimension. The crystals belong to space group R32 with a = b = 244.3 A and c = 920.9 A (hexagonal setting), and have a solvent content of 73%. The asymmetric unit contains one-third of the molecule, i.e., 20 of the 60 subunits. Initial X-ray crystallographic data to 7 A resolution were collected at cryotemperatures at synchrotron facilities. Interestingly, the diffraction was improved significantly upon rehydrating dehydrated crystals and extended to 4.2 A.
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T. Izard, A. Aevarsson, M. D. Allen, A. H. Westphal, R. N. Perham, A. de Kok, and W. G. J. Hol
Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes
PNAS, February 16, 1999; 96(4): 1240 - 1245.
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