Evidence map›Paper›PMID 38013689›Full record

ArticlePure and applied chemistry. Chimie pure et appliquee2023

Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs.

Isabel Bogacz, Hiroki Makita, Philipp S Simon, Miao Zhang, Margaret D Doyle, Ruchira Chatterjee, Thomas Fransson, Clemens Weninger, Franklin Fuller, Leland Gee and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Pure and applied chemistry. Chimie pure et appliquee, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

17 authors.

Isabel BogaczMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0003-1493-3867
Hiroki MakitaMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-4968-914X
Philipp S SimonMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-2859-4475
Miao ZhangMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0003-4022-7093
Margaret D DoyleMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-7289-3544
Ruchira ChatterjeeMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-0865-061X
Thomas FranssonDepartment of Theoretical chemistry and Biology, KTH Royal Institute of Technology, Stockholm, Sweden.ORCID https://orcid.org/0000-0002-3770-9780
Clemens WeningerMAX IV Laboratory, Lund University, Lund, Sweden.ORCID https://orcid.org/0000-0002-7453-7914
Franklin FullerLCLS, SLAC National Accelerator Laboratory, 94025, Menlo Park, CA, USA.ORCID https://orcid.org/0000-0002-3773-7087
Leland GeeLCLS, SLAC National Accelerator Laboratory, 94025, Menlo Park, CA, USA.ORCID https://orcid.org/0000-0002-5817-3997
Takahiro SatoLCLS, SLAC National Accelerator Laboratory, 94025, Menlo Park, CA, USA.ORCID https://orcid.org/0000-0003-2202-0910
Matthew SeabergLCLS, SLAC National Accelerator Laboratory, 94025, Menlo Park, CA, USA.ORCID https://orcid.org/0000-0002-4560-4698
Roberto Alonso-MoriLCLS, SLAC National Accelerator Laboratory, 94025, Menlo Park, CA, USA.ORCID https://orcid.org/0000-0002-5357-0934
Uwe BergmannDepartment of Physics, University of Wisconsin-Madison, 53706, Madison, WI, USA.ORCID https://orcid.org/0000-0001-5639-166X
Vittal K YachandraMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-3983-7858
Jan KernMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0002-7272-1603
Junko YanoMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720, Berkeley, CA, USA.ORCID https://orcid.org/0000-0001-6308-9071

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
Structural Dynamics at LCLSP41GM139687 · NIGMS · STANFORD UNIVERSITY · PI HUNTER, MARK · 2021 to 2025
$7.5M
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
High throughput sample delivery method for time resolved studies of enzyme reactions with X-ray and complementary techniquesR01GM126289 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KERN, JAN F · 2017 to 2025
$4.6M
Taking Snapshots of Enzymatic Reactions Using X-ray Crystallography and SpectroscopyR35GM149528 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI VITTAL YACHANDRA · 2023 to 2026
$2.7M
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 P41 GM139687NIGMS NIH HHS R01 GM055302NIGMS NIH HHS R01 GM110501NIGMS NIH HHS R01 GM126289NIGMS NIH HHS R35 GM149528NIGMS NIH HHS R56 GM055302
6 · The paper itself

Abstract

X-ray crystallography and X-ray spectroscopy using X-ray free electron lasers plays an important role in understanding the interplay of structural changes in the protein and the chemical changes at the metal active site of metalloenzymes through their catalytic cycles. As a part of such an effort, we report here our recent development of methods for X-ray absorption spectroscopy (XAS) at XFELs to study dilute biological samples, available in limited volumes. Our prime target is Photosystem II (PS II), a multi subunit membrane protein complex, that catalyzes the light-driven water oxidation reaction at the Mn

Indexed as

ManganesePhotoIUPAC 2022photosystem IIwater oxidationX-ray absorption spectroscopyX-ray free electron lasers

Identifiers

PMID38013689
PMCPMC10505480

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.