Evidence map›Paper›PMID 22919444›Full record

ArticleThe journal of physical chemistry letters2012

Fast Detection Allows Analysis of the Electronic Structure of Metalloprotein by X-ray Emission Spectroscopy at Room Temperature.

Katherine M Davis, Brian A Mattern, Joseph I Pacold, Taisiya Zakharova, Dale Brewe, Irina Kosheleva, Robert W Henning, Timothy J Graber, Steve M Heald, Gerald T Seidler and 1 more

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. AXSIS: Exploring the frontiers in attosecond X-ray science, imaging and spectroscopy.Nuclear instruments & methods in physics research. Section A, Accelerators, spectrometers, detectors and associated equipment · 2016
    Article
  6. Article
  7. Article
  8. Kinetic modeling of the X-ray-induced damage to a metalloprotein.The journal of physical chemistry. B · 2013
    Article
  9. Article
  10. 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

11 authors at 4 institutions in 1 country.

Katherine M DavisDepartment of Physics, Purdue University, West Lafayette, IN 47907, USA.
Brian A Mattern
Joseph I Pacold
Taisiya Zakharova
Dale Brewe
Irina Kosheleva
Robert W Henning
Timothy J Graber
Steve M Heald
Gerald T Seidler
Yulia Pushkar
Purdue University West Lafayette · USUniversity of Chicago · USUniversity of Washington · USArgonne National Laboratory · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
BioCARS: A Synchroton Structural Biology ResourceP41GM103543 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2012 to 2012
$1.1M
NCRR NIH HHS P41 RR007707NIGMS NIH HHS P41 GM103543
6 · The paper itself

Abstract

The paradigm of "detection-before-destruction" was tested for a metalloprotein complex exposed at room temperature to the high x-ray flux typical of third generation synchrotron sources. Following the progression of the x-ray induced damage by Mn Kβ x-ray emission spectroscopy, we demonstrated the feasibility of collecting room temperature data on the electronic structure of native Photosystem II, a trans-membrane metalloprotein complex containing a Mn(4)Ca cluster. The determined non-damaging observation timeframe (about 100 milliseconds using continuous monochromatic beam, deposited dose 1*10(7) photons/µm(2) or 1.3*10(4) Gy, and 66 microseconds in pulsed mode using pink beam, deposited dose 4*10(7) photons/µm(2) or 4.2*10(4) Gy) is sufficient for the analysis of this protein's electron dynamics and catalytic mechanism at room temperature. Reported time frames are expected to be representative for other metalloproteins. The described instrumentation, based on the short working distance dispersive spectrometer, and experimental methodology is broadly applicable to time-resolved x-ray emission analysis at synchrotron and x-ray free-electron laser light sources.

Identifiers

PMID22919444
PMCPMC3423219
OpenAlexW287408891

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.