Evidence map›Paper›PMID 27262052›Full record

ArticleProtein science : a publication of the Protein Society2016

Destruction-and-diffraction by X-ray free-electron laser.

Jimin Wang

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Oxygen additions in serial femtosecond crystallographic protein structures.Protein science : a publication of the Protein Society · 2016
    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

1 author.

Jimin WangDepartment of Molecular Biophysics and Biochemistry, Yale University, Connecticut 06520, New Haven.

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
NIGMS NIH HHS P01 GM022778
6 · The paper itself

Abstract

It is common knowledge that macromolecular crystals are damaged by the X-rays they are exposed to during conventional data collection. One of the claims made about the crystallographic data collection now being collected using X-ray free-electron lasers (XFEL) is that they are unaffected by radiation damage. XFEL data sets are assembled by merging data obtained from a very large number of crystals, each of which is exposed to a single femtosecond pulse of radiation, the duration of which is so short that diffraction occurs before the damage done to the crystal has time to become manifest, i.e. "diffraction-before-destruction." However, recent theoretical studies have shown that many of the elemental electronic processes that ultimately result in the destruction of such crystals occur during a single pulse. It is predicted that the amplitudes of atomic scattering factor could be reduced by as much as 75% within the first 5 femtoseconds of such pulses, and that different atoms will respond in different ways. Experimental evidence is provided here that these predictions are correct.

Indexed as

ElectronsLasersScattering, RadiationCytochrome-c PeroxidaseElectron Transport Complex IVPhotosystem II Protein ComplexProtein DomainsCytochrome-c PeroxidaseElectron Transport Complex IVPhotosystem II Protein Complexatomic scattering factorscytochrome c oxidasecytochrome c peroxidasemetalloproteinsphotosystem IIradiation damageXFEL

Identifiers

PMID27262052
PMCPMC5338243

What OpenQuestion holds

Textmetadata
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.