Abstract
The enzyme diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is capable of decontaminating a wide variety of toxic organophosphorus nerve agents. DFPase is structurally related to a number of enzymes, such as the medically important paraoxonase (PON). In order to investigate the reaction mechanism of this phosphotriesterase and to elucidate the protonation state of the active-site residues, large-sized crystals of DFPase have been prepared for neutron diffraction studies. Available H atoms have been exchanged through vapour diffusion against D2O-containing mother liquor in the capillary. A neutron data set has been collected to 2.2 Å resolution on a relatively small (0.43 mm3) crystal at the spallation source in Los Alamos. The sample size and asymmetric unit requirements for the feasibility of neutron diffraction studies are summarized.
Original language | English |
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Pages (from-to) | 42-45 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 63 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2007 |
Externally published | Yes |
Keywords
- DFPase
- Neutron diffraction
- Phosphotriesterase
- Time-of-flight