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Atomic resolution crystal structure of squid ganglion DFPase by Juergen Koepke; Eileen I. Scharff; Christian Lücke; Heinz Rüterjans; Günter Fritzsch is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Diisopropylfluorophosphatases (DFP-ases) are capable of detoxifying chemical warfare agents like diisopropylfluorophosphate (DFP) by hydrolysis. The protein reported here was recombinantely expressed in __E. coli__. The X-ray cystal structure of this enzyme has been refined to a resolution of 0.85 Å and a crystallographic R value of 9.4%. Reversible flash-cooling improved both, mosaicity and resolution of the crystals considerably. The overall structure of this protein represents a six-bladed β-propeller with two calcium ions bound in a central water filled tunnel. 496 water, 2 glycerol, 2 MES-buffer molecules, and 18 PEG fragments of different lengths could be refined in the solvent region. The 208 most reliable residues, without disorder or reduced occupancy in their side-chains, were finally refined without restraints. A subsequent full-matrix refinement cycle for the positional parameters yielded estimated standard deviations (esds) by matrix inversion. The herewith calculated bond lenghts and bond-esds were used to obtain averaged bond lengths, which have been compared to the restraints used in preceding refinement cycles.

Who reads Atomic resolution crystal structure of squid ganglion DFPase?

Author

Juergen Koepke; Eileen I. Scharff; Christian Lücke; Heinz Rüterjans; Günter Fritzsch

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)