Evidence map›Paper›PMID 27377382›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Second harmonic generation correlation spectroscopy for characterizing translationally diffusing protein nanocrystals.

Ximeng Y Dow, Christopher M Dettmar, Emma L DeWalt, Justin A Newman, Alexander R Dow, Shatabdi Roy-Chowdhury, Jesse D Coe, Christopher Kupitz, Petra Fromme, Garth J Simpson

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. 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. Depth-of-field extension in optical imaging for rapid crystal screening.Acta crystallographica. Section D, Structural biology · 2021
    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

10 authors.

Ximeng Y DowChemistry Department, Purdue University, West Lafayette, IN 47907, USA.
Christopher M DettmarChemistry Department, Purdue University, West Lafayette, IN 47907, USA.
Emma L DeWaltChemistry Department, Purdue University, West Lafayette, IN 47907, USA.
Justin A NewmanChemistry Department, Purdue University, West Lafayette, IN 47907, USA.
Alexander R DowChemistry Department, Purdue University, West Lafayette, IN 47907, USA.
Shatabdi Roy-ChowdhurySchool of Molecular Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Jesse D CoeSchool of Molecular Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Christopher KupitzSchool of Molecular Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Petra FrommeSchool of Molecular Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Garth J SimpsonChemistry Department, Purdue University, West Lafayette, IN 47907, USA.

Funding

Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
Nonlinear Optical Imaging for Guiding Protein Structure DeterminationR01GM103401 · NIGMS · PURDUE UNIVERSITY · PI SIMPSON, GARTH JASON · 2012 to 2018
$1.7M
Ultrafast Nonlinear Optical Approaches toward High-Throughput Membrane Protein NaR01GM103910 · NIGMS · PURDUE UNIVERSITY · PI SIMPSON, GARTH JASON · 2013 to 2016
$1.1M
NIGMS NIH HHS R01 GM095583NIGMS NIH HHS R01 GM103401NIGMS NIH HHS R01 GM103910
6 · The paper itself

Abstract

Second harmonic generation correlation spectroscopy (SHG-CS) is demonstrated as a new approach to protein nanocrystal characterization. A novel line-scanning approach was performed to enable autocorrelation analysis without sample damage from the intense incident beam. An analytical model for autocorrelation was developed, which includes a correction for the optical scattering forces arising when focusing intense, infrared beams. SHG-CS was applied to the analysis of BaTiO3 nanoparticles ranging from 200 to ∼500 nm and of photosystem I nanocrystals. A size distribution was recovered for each sample and compared with the size histogram measured by scanning electron microscopy (SEM). Good agreement was observed between the two independent measurements. The intrinsic selectivity of the second-order nonlinear optical process provides SHG-CS with the ability to distinguish well ordered nanocrystals from conglomerates and amorphous aggregates. Combining the recovered distribution of particle diameters with the histogram of measured SHG intensities provides the inherent hyperpolarizability per unit volume of the SHG-active nanoparticles. Simulations suggest that the SHG activity per unit volume is likely to exhibit relatively low sensitivity to the subtle distortions within the lattice that contribute to resolution loss in X-ray diffraction, but high sensitivity to the presence of multi-domain crystals.

Indexed as

Bacterial ProteinsBarium CompoundsCrystallizationDiffusionInfrared RaysMicroscopy, Electron, ScanningNanoparticlesOptical PhenomenaPhotosystem I Protein ComplexSpectrum AnalysisSynechococcusTitaniumBacterial ProteinsBarium Compoundsbarium titanate(IV)Photosystem I Protein ComplexTitaniumcorrelation spectroscopyprotein nanocrystalssecond harmonic generationsize distributionXFEL

Identifiers

PMID27377382
PMCPMC4932918

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.