Evidence map›Paper›PMID 26342144›Full record

ReviewCurrent opinion in structural biology2015

Metalloprotein structures at ambient conditions and in real-time: biological crystallography and spectroscopy using X-ray free electron lasers.

Jan Kern, Vittal K Yachandra, Junko Yano

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.7field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Radiation damage in protein crystallography at X-ray free-electron lasers.Acta crystallographica. Section D, Structural biology · 2019
    Review
  17. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  18. Review
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Jan KernPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA. Electronic address: JFKern@LBL.GOV.
Vittal K YachandraPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: VKYachandra@LBL.GOV.
Junko YanoPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: JYano@LBL.GOV.
Lawrence Berkeley National Laboratory · USSLAC National Accelerator Laboratory · US

Funding

Taking Snapshots of the Water-Oxidation Reaction by the Mn4Ca Oxygen-Evolving Complex Using X-ray Crystallography and SpectroscopyR01GM055302 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI YACHANDRA, VITTAL · 1997 to 2022
$9.1M
Biological Spectroscopy and Crystallography Using an X-ray Free Electron Laser - Supplemental EquipmentR01GM110501 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Junko Yano · 2014 to 2026
$4.8M
Structure and Function of the Mn Oxygen-Evolving ComplexR56GM055302 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI YACHANDRA, VITTAL · 2009 to 2009
$530k
NIGMS NIH HHS GM110501NIGMS NIH HHS GM55302NIGMS NIH HHS R01 GM055302NIGMS NIH HHS R01 GM110501NIGMS NIH HHS R56 GM055302
6 · The paper itself

Abstract

Although the structure of enzymes and the chemistry at the catalytic sites have been studied intensively, an understanding of the atomic-scale chemistry requires a new approach beyond steady state X-ray crystallography and X-ray spectroscopy at cryogenic temperatures. Following the dynamic changes in the geometric and electronic structure of metallo-enzymes at ambient conditions, while overcoming the severe X-ray-induced changes to the redox active catalytic center, is key for deriving reaction mechanisms. Such studies become possible by the intense and ultra-short femtosecond (fs) X-ray pulses from an X-ray free electron laser (XFEL) by acquiring a signal before the sample is destroyed. This review describes the recent and pioneering uses of XFELs to study the protein structure and dynamics of metallo-enzymes using crystallography and scattering, as well as the chemical structure and dynamics of the catalytic complexes (charge, spin, and covalency) using spectroscopy during the reaction to understand the electron-transfer processes and elucidate the mechanism.

Indexed as

Models, MolecularProtein ConformationBinding SitesCrystallography, X-RayLasersMetalloproteinsMetalsProtein BindingSpectrum AnalysisTemperatureMetalloproteinsMetals

Identifiers

PMID26342144
PMCPMC4821593
OpenAlexW1210608600

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.