Evidence map›Paper›PMID 25849493›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Large-volume protein crystal growth for neutron macromolecular crystallography.

Joseph D Ng, James K Baird, Leighton Coates, Juan M Garcia-Ruiz, Teresa A Hodge, Sijay Huang

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 44 citations in OpenAlex.

  1. Flow as a Control Strategy to Promote Biomolecule Nucleation.Advances in biochemical engineering/biotechnology · 2026
    Review
  2. Article
  3. Article
  4. Improved joint X-ray and neutron refinement procedure in Phenix.Acta crystallographica. Section D, Structural biology · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Semi-empirical model to estimate ideal conditions for the growth of large protein crystals.Acta crystallographica. Section D, Structural biology · 2020
    Article
  13. Article
  14. Review
  15. Protein crystallization and initial neutron diffraction studies of the photosystem II subunit PsbO.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  16. Review
  17. 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

6 authors at 4 institutions in 2 countries.

Joseph D NgDepartment of Biological Sciences, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
James K BairdDepartment of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
Leighton CoatesBiology and Soft Matter Division, Oak Ridge National Laboratory, PO Box 2008, MS6475, Oak Ridge, TN 37831, USA.
Juan M Garcia-RuizLaboratorio de Estudios Cristalográficos (IACT), CSIC-Universidad de Granada, Avenida de la Innovación s/n, Armilla (Granada), Spain.
Teresa A HodgeDepartment of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
Sijay HuangDepartment of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
University of Alabama in Huntsville · USiXpressGenes (United States) · USOak Ridge National Laboratory · USUniversidad de Granada · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neutron macromolecular crystallography (NMC) is the prevailing method for the accurate determination of the positions of H atoms in macromolecules. As neutron sources are becoming more available to general users, finding means to optimize the growth of protein crystals to sizes suitable for NMC is extremely important. Historically, much has been learned about growing crystals for X-ray diffraction. However, owing to new-generation synchrotron X-ray facilities and sensitive detectors, protein crystal sizes as small as in the nano-range have become adequate for structure determination, lessening the necessity to grow large crystals. Here, some of the approaches, techniques and considerations for the growth of crystals to significant dimensions that are now relevant to NMC are revisited. These include experimental strategies utilizing solubility diagrams, ripening effects, classical crystallization techniques, microgravity and theoretical considerations.

Indexed as

CrystallizationCrystallographyMacromolecular SubstancesNeutron DiffractionProteinsMacromolecular SubstancesProteinslarge-volume crystalsneutron macromolecular crystallography

Identifiers

PMID25849493
PMCPMC4388167
OpenAlexW2003978675

What OpenQuestion holds

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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.