Evidence map›Paper›PMID 25084371›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Identifying, studying and making good use of macromolecular crystals.

Guillermo Calero, Aina E Cohen, Joseph R Luft, Janet Newman, Edward H Snell

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Moving beyond MARCO.PloS one · 2023
    Article
  3. Review
  4. Article
  5. Macromolecular crystallography using microcrystal electron diffraction.Acta crystallographica. Section D, Structural biology · 2021
    Review
  6. Article
  7. Article
  8. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  9. Article
  10. Transmission electron microscopy for the evaluation and optimization of crystal growth.Acta crystallographica. Section D, Structural biology · 2016
    Article
  11. Article
  12. Article
  13. Exploiting Microbeams for Membrane Protein Structure Determination.Advances in experimental medicine and biology
    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

5 authors.

Guillermo CaleroDepartment of Structural Biology, University of Pittsburgh Medical School, Pittsburgh, PA 15261, USA.
Aina E CohenStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, USA.
Joseph R LuftHauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY 14203, USA.
Janet NewmanCSIRO Collaborative Crystallisation Centre, 343 Royal Parade, Parkville, Victoria 3052, Australia.
Edward H SnellHauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY 14203, USA.

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Structural and Functional Mechanisms of PTH-Receptor SignalingR01DK102495 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO, GARDELLA, THOMAS J · 2014 to 2017
$2.0M
Enabling Technologies to Macromolecular CrystallizationR01GM100494 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI LUFT, JOSEPH · 2011 to 2014
$1.9M
Development of an Expert Crystallization Knowledge SystemR01GM088396 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI SNELL, EDWARD H · 2010 to 2014
$1.7M
NIDDK NIH HHS R01 DK102495NIDDK NIH HHS R01DK102495NIGMS NIH HHS GM100494NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM088396NIGMS NIH HHS R01GM088396NIGMS NIH HHS R01 GM100494
6 · The paper itself

Abstract

Structural biology has contributed tremendous knowledge to the understanding of life on the molecular scale. The Protein Data Bank, a depository of this structural knowledge, currently contains over 100,000 protein structures, with the majority stemming from X-ray crystallography. As the name might suggest, crystallography requires crystals. As detectors become more sensitive and X-ray sources more intense, the notion of a crystal is gradually changing from one large enough to embellish expensive jewellery to objects that have external dimensions of the order of the wavelength of visible light. Identifying these crystals is a prerequisite to their study. This paper discusses developments in identifying these crystals during crystallization screening and distinguishing them from other potential outcomes. The practical aspects of ensuring that once a crystal is identified it can then be positioned in the X-ray beam for data collection are also addressed.

Indexed as

CrystallizationMacromolecular SubstancesCrystallography, X-RayMacromolecular Substancescrystal detectioncrystal growthcrystal positioning

Identifiers

PMID25084371
PMCPMC4118793

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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.