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Atomic resolution crystal structure of squid ganglion DFPase

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Koepke,  J.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Fritzsch,  G.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Koepke, J., Scharff, E. I., Lücke, C., Rüterjans, H., & Fritzsch, G. (2002). Atomic resolution crystal structure of squid ganglion DFPase. Acta Crystallographica Section D-Biological Crystallography, 58(Part 10 Special Issue 1), 1757-1759.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-DC7C-7
Abstract
Diisopropylfluorophosphatases (DFP-ases) are capable of detoxifying chemical warfare agents like diisopropyl fluorophosphate (DFP) by hydrolysis. The protein reported here was recombinantly expressed in E. coli. The X-ray crystal structure of this enzyme has been refined to a resolution of 0.85 Angstrom 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 beta-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 lengths and bond-esds were used to obtain averaged bond lengths, which have been compared to the restraints used in preceding refinement cycles. [References: 20]