Evidence map›Paper›PMID 24311594›Full record

ArticleActa crystallographica. Section D, Biological crystallography2013

Protein energy landscapes determined by five-dimensional crystallography.

Marius Schmidt, Vukica Srajer, Robert Henning, Hyotcherl Ihee, Namrta Purwar, Jason Tenboer, Shailesh Tripathi

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

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  18. Best practices for time-resolved serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2022
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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

7 authors.

Marius SchmidtPhysics Department, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA.
Vukica Srajer
Robert Henning
Hyotcherl Ihee
Namrta Purwar
Jason Tenboer
Shailesh Tripathi

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 Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
BioCARS: A Synchroton Structural Biology ResourceP41GM103543 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2012 to 2012
$1.1M
NCRR NIH HHS P41 RR007707NCRR NIH HHS P41RR007707NIGMS NIH HHS P41 GM103543NIGMS NIH HHS P41GM103543NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

Free-energy landscapes decisively determine the progress of enzymatically catalyzed reactions [Cornish-Bowden (2012), Fundamentals of Enzyme Kinetics, 4th ed.]. Time-resolved macromolecular crystallography unifies transient-state kinetics with structure determination [Moffat (2001), Chem. Rev. 101, 1569-1581; Schmidt et al. (2005), Methods Mol. Biol. 305, 115-154; Schmidt (2008), Ultrashort Laser Pulses in Medicine and Biology] because both can be determined from the same set of X-ray data. Here, it is demonstrated how barriers of activation can be determined solely from five-dimensional crystallography, where in addition to space and time, temperature is a variable as well [Schmidt et al. (2010), Acta Cryst. A66, 198-206]. Directly linking molecular structures with barriers of activation between them allows insight into the structural nature of the barrier to be gained. Comprehensive time series of crystallographic data at 14 different temperature settings were analyzed and the entropy and enthalpy contributions to the barriers of activation were determined. One hundred years after the discovery of X-ray scattering, these results advance X-ray structure determination to a new frontier: the determination of energy landscapes.

Indexed as

ThermodynamicsBacteriaBacterial ProteinsCrystallography, X-RayKineticsPhotoreceptors, MicrobialProtein ConformationBacterial Proteinsphotoactive yellow protein, BacteriaPhotoreceptors, Microbialchemical kineticsfive-dimensional crystallographyphotoactive yellow proteintime-resolved crystallographytime-resolved microspectrophotometry

Identifiers

PMID24311594
PMCPMC3852658

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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.