Evidence map›Paper›PMID 29354268›Full record

ArticleIUCrJ2018

An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase.

Thomas P Halsted, Keitaro Yamashita, Kunio Hirata, Hideo Ago, Go Ueno, Takehiko Tosha, Robert R Eady, Svetlana V Antonyuk, Masaki Yamamoto, S Samar Hasnain

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Synchrotron science in the UK: NINA, the SRS and Diamond.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019
    Article
  14. Article
  15. Review
  16. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
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

10 authors at 2 institutions in 2 countries.

Thomas P HalstedMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.ORCID https://orcid.org/0000-0002-5977-6511
Keitaro YamashitaSR Life Science Instrumentation Unit, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.ORCID https://orcid.org/0000-0002-5442-7582
Kunio HirataSR Life Science Instrumentation Unit, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.
Hideo AgoSR Life Science Instrumentation Unit, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.
Go UenoSR Life Science Instrumentation Unit, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.ORCID https://orcid.org/0000-0001-7718-0327
Takehiko ToshaBiometal Science Laboratory, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.ORCID https://orcid.org/0000-0002-8971-0759
Robert R EadyMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.
Svetlana V AntonyukMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.ORCID https://orcid.org/0000-0002-2779-9946
Masaki YamamotoSR Life Science Instrumentation Unit, RIKEN SPring-8 Centre, Sayo 679-5148, Japan.ORCID https://orcid.org/0000-0002-1311-1768
S Samar HasnainMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.ORCID https://orcid.org/0000-0002-2854-4718
SPring-8 · JPUniversity of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synchrotron-based X-ray structural studies of ligand-bound enzymes are powerful tools to further our understanding of reaction mechanisms. For redox enzymes, it is necessary to study both the oxidized and reduced active sites to fully elucidate the reaction, an objective that is complicated by potential X-ray photoreduction. In the presence of the substrate, this can be exploited to construct a structural movie of the events associated with catalysis. Using the newly developed approach of serial femtosecond rotation crystallography (SF-ROX), an X-ray damage-free structure of the as-isolated copper nitrite reductase (CuNiR) was visualized. The sub-10 fs X-ray pulse length from the SACLA X-ray free-electron laser allowed diffraction data to be collected to 1.6 Å resolution in a 'time-frozen' state. The extremely short duration of the X-ray pulses ensures the capture of data prior to the onset of radiation-induced changes, including radiolysis. Unexpectedly, an O

Indexed as

copper nitrite reductaseO2 bindingserial femtosecond rotation crystallography

Identifiers

PMID29354268
PMCPMC5755574
OpenAlexW2770356627

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.