X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.

作者: Marc-Michael Blum , Stephen J. Tomanicek , Harald John , B. Leif Hanson , Heinz Rüterjans

DOI: 10.1107/S1744309110004318

关键词:

摘要: The signal-to-noise ratio is one of the limiting factors in neutron macromolecular crystallography. Protein perdeuteration, which replaces all H atoms with deuterium, a method improving crystallography experiments by reducing incoherent scattering hydrogen isotope. Detailed analyses perdeuterated and hydrogenated structures are necessary order to evaluate utility crystals for diffraction studies. room-temperature X-ray structure diisopropyl fluorophosphatase (DFPase) reported at 2.1 A resolution. Comparison an independently refined DFPase revealed no major systematic differences, although did not diffract neutrons. lack examined respect data-collection crystallo­graphic parameters. characteristics successful determinations presented as guideline future studies macromolecules. beyond 2.0 A resolution appears be strong predictor structures.

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