Evidence map›Paper›PMID 37223996›Full record

ArticleIUCrJ2023

Design and implementation of suspended drop crystallization.

Cody Gillman, William J Nicolas, Michael W Martynowycz, Tamir Gonen

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Reaching the potential of electron diffraction.Cell reports. Physical science · 2024
    Article
  8. Article
  9. Applying 3D ED/MicroED workflows toward the next frontiers.Acta crystallographica. Section C, Structural chemistry · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Cody GillmanDepartments of Biological Chemistry and Physiology, University of California, Los Angeles, CA, USA.
William J NicolasDepartments of Biological Chemistry and Physiology, University of California, Los Angeles, CA, USA.
Michael W MartynowyczDepartments of Biological Chemistry and Physiology, University of California, Los Angeles, CA, USA.
Tamir GonenDepartments of Biological Chemistry and Physiology, University of California, Los Angeles, CA, USA.
Howard Hughes Medical Institute · USUniversity of California, Los Angeles · US

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
Muscle Cell Biology, Pathophysiology, and TherapeuticsT32AR065972 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Rachelle Hope Crosbie, THOMAS A. RANDO · 2016 to 2026
$3.9M
NIAMS NIH HHS T32 AR065972NIGMS NIH HHS P41 GM136508
6 · The paper itself

Abstract

In this work, a novel crystal growth method termed suspended drop crystallization has been developed. Unlike traditional methods, this technique involves mixing protein and precipitant directly on an electron microscopy grid without any additional support layers. The grid is then suspended within a crystallization chamber designed in-house, allowing for vapor diffusion to occur from both sides of the drop. A UV-transparent window above and below the grid enables the monitoring of crystal growth via light, UV or fluorescence microscopy. Once crystals have formed, the grid can be removed and utilized for X-ray crystallography or microcrystal electron diffraction (MicroED) directly without having to manipulate the crystals. To demonstrate the efficacy of this method, crystals of the enzyme proteinase K were grown and its structure was determined by MicroED following focused ion beam/scanning electron microscopy milling to render the sample thin enough for cryoEM. Suspended drop crystallization overcomes many of the challenges associated with sample preparation, providing an alternative workflow for crystals embedded in viscous media, sensitive to mechanical stress and/or subject to preferred orientation on electron microscopy grids.

Indexed as

ProteinsCryoelectron MicroscopyCrystallizationCrystallography, X-RayEndopeptidase KEndopeptidase KProteins3D printingCryoEMcryogenic freezingFIB millingFIB/SEMmembrane proteinsmicrocrystal electron diffractionMicroEDstructural studies of nano-/microcrystalsTEM

Identifiers

PMID37223996
PMCPMC10324482
OpenAlexW4378072192

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.