Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris

Marc Michael Blum, Alexander Koglin, Heinz Rüterjans, Benno Schoenborn, Paul Langan, Julian C.H. Chen

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

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 languageEnglish
Pages (from-to)42-45
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number1
DOIs
StatePublished - Jan 2007
Externally publishedYes

Keywords

  • DFPase
  • Neutron diffraction
  • Phosphotriesterase
  • Time-of-flight

Fingerprint

Dive into the research topics of 'Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris'. Together they form a unique fingerprint.

Cite this