Evidence map›Paper›PMID 33490105›Full record

ArticleFrontiers in molecular biosciences2020

Rapid Structural Analysis of a Synthetic Non-canonical Amino Acid by Microcrystal Electron Diffraction.

Patrick R Gleason, Brent L Nannenga, Jeremy H Mills

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. MicroED in drug discovery.Current opinion in structural biology · 2023
    Review
  3. Review
  4. 3D Electron Diffraction Structure Determination of Terrylene, a Promising Candidate for Intermolecular Singlet Fission.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  5. 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

3 authors.

Patrick R GleasonSchool of Molecular Sciences, Arizona State University, Tempe, AZ, United States.
Brent L NannengaChemical Engineering, School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, United States.
Jeremy H MillsSchool of Molecular Sciences, Arizona State University, Tempe, AZ, United States.

Funding

TRD4: Design and Engineering of MicroED hardware for nanocrystallization and time resolved studiesP41GM136508 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GONEN, TAMIR · 2020 to 2024
$7.6M
Structure Determination of G Protein-Coupled Receptors by Microcrystal Electron DiffractionR01GM124152 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI NANNENGA, BRENT · 2017 to 2021
$1.6M
Expanding the fluorescent toolkit with non-canonical amino acidsR01GM136996 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI MILLS, JEREMY · 2020 to 2023
$1.4M
Genetically encodable epitopes to overcome size and resolution limits in cryo-EMR21GM131299 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI MILLS, JEREMY, NANNENGA, BRENT · 2019 to 2020
$430k
NIGMS NIH HHS P41 GM136508NIGMS NIH HHS R01 GM124152NIGMS NIH HHS R01 GM136996NIGMS NIH HHS R21 GM131299
6 · The paper itself

Abstract

Structural characterization of small molecules is a crucial component of organic synthesis. In this work, we applied microcrystal electron diffraction (MicroED) to analyze the structure of the product of an enzymatic reaction that was intended to produce the unnatural amino acid 2,4-dihydroxyphenylalanine (24DHF). Characterization of our isolated product with nuclear magnetic resonance spectroscopy (NMR) and mass spectrometry (MS) suggested that an isomer of 24DHF had been formed. Microcrystals present in the isolated product were then used to determine its structure to 0.62 Å resolution, which confirmed its identity as 2-amino-2-(2,4-dihydroxyphenyl)propanoic acid (24DHPA). Moreover, the MicroED structural model indicated that both enantiomeric forms of 24DHPA were present in the asymmetric unit. Notably, the entire structure determination process including setup, data collection, and refinement was completed in ~1 h. The MicroED data not only bolstered previous results obtained using NMR and MS but also immediately provided information about the stereoisomers present in the product, which is difficult to achieve using NMR and MS alone. Our results therefore demonstrate that MicroED methods can provide useful structural information on timescales that are similar to many commonly used analytical methods and can be added to the existing suite of small molecule structure determination tools in future studies.

Indexed as

electron diffractionmicrocrystal electron diffraction (MicroED)non-canonical amino acid (ncAA)organic synthesistransmission electron microscope (TEM)

Identifiers

PMID33490105
PMCPMC7821094

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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.