Title : Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris - Blum_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_42 |
Author(s) : Blum MM , Koglin A , Ruterjans H , Schoenborn B , Langan P , Chen JC |
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :42 , 2007 |
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. |
PubMedSearch : Blum_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_42 |
PubMedID: 17183172 |
Blum MM, Koglin A, Ruterjans H, Schoenborn B, Langan P, Chen JC (2007)
Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :42
Blum MM, Koglin A, Ruterjans H, Schoenborn B, Langan P, Chen JC (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :42