Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 63(Pt 1): 42-5, 2007 Jan 01.
Article
in En
| MEDLINE
| ID: mdl-17183172
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 A 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Neutron Diffraction
/
Phosphoric Triester Hydrolases
/
Loligo
Limits:
Animals
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2007
Document type:
Article
Affiliation country:
Germany