Evidence map›Paper›PMID 20383004›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

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

Marc Michael Blum, Stephen J Tomanicek, Harald John, B Leif Hanson, Heinz Rüterjans, Benno P Schoenborn, Paul Langan, Julian C H Chen

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  5. High-resolution X-ray study of the effects of deuteration on crystal growth and the crystal structure of proteinase K.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  6. Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).Acta crystallographica. Section D, Biological crystallography · 2010
    Article
  7. Joint X-ray and neutron refinement with phenix.refine.Acta crystallographica. Section D, Biological crystallography · 2010
    Article
  8. Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase).Acta crystallographica. Section D, Biological crystallography · 2010
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Marc Michael BlumBlum Scientific Services, Ledererstrasse 23, 80331 Munich, Germany.
Stephen J Tomanicek
Harald John
B Leif Hanson
Heinz Rüterjans
Benno P Schoenborn
Paul Langan
Julian C H Chen
University of Toledo · USGoethe University Frankfurt · DELos Alamos National Laboratory · USUniversität der Bundeswehr München · DE

Funding

Computational Tools for Neutron Protein CrystallographyR01GM071939 · NIGMS · UT-BATTELLE, LLC-OAK RIDGE NATIONAL LAB · PI COATES, LEIGHTON · 2004 to 2019
$4.3M
NIGMS NIH HHS 1R01GM071939-01NIGMS NIH HHS R01 GM071939
6 · The paper itself

Abstract

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

Indexed as

AnimalsCrystallography, X-RayDecapodiformesModels, MolecularNeutron DiffractionPhosphoric Triester HydrolasesProtein Structure, Tertiarydiisopropyl-fluorophosphatasePhosphoric Triester Hydrolases

Identifiers

PMID20383004
PMCPMC2852326
OpenAlexW2019015056

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.