Evidence map›Paper›PMID 25372810›Full record

ReviewActa crystallographica. Section F, Structural biology communications2014

Optimization of crystallization conditions for biological macromolecules.

Alexander McPherson, Bob Cudney

Abstract readReview
In one paragraph

Review 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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Crystallization and 1.6 Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  3. Article
  4. Article
  5. Investigating Potential 5' UTR G-Quadruplexes Within NRF2 mRNA.Current issues in molecular biology · 2026
    Article
  6. Article
  7. Phase Diagrams as a DOE Tool in Biomolecular Crystallization.Advances in biochemical engineering/biotechnology · 2026
    Review
  8. Biomolecular Crystallisation Through Soft Templates and Seeding.Advances in biochemical engineering/biotechnology · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. PDBe tools for an in-depth analysis of small molecules in the Protein Data Bank.Protein science : a publication of the Protein Society · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The FUSION protein crystallization screen.Journal of applied crystallography · 2022
    Article
  19. Article
  20. 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

2 authors.

Alexander McPhersonDepartment of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697, USA.
Bob CudneyHampton Research, 34 Journey, Aliso Viejo, CA 92656-3317, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the successful X-ray structure determination of macromolecules, it is first necessary to identify, usually by matrix screening, conditions that yield some sort of crystals. Initial crystals are frequently microcrystals or clusters, and often have unfavorable morphologies or yield poor diffraction intensities. It is therefore generally necessary to improve upon these initial conditions in order to obtain better crystals of sufficient quality for X-ray data collection. Even when the initial samples are suitable, often marginally, refinement of conditions is recommended in order to obtain the highest quality crystals that can be grown. The quality of an X-ray structure determination is directly correlated with the size and the perfection of the crystalline samples; thus, refinement of conditions should always be a primary component of crystal growth. The improvement process is referred to as optimization, and it entails sequential, incremental changes in the chemical parameters that influence crystallization, such as pH, ionic strength and precipitant concentration, as well as physical parameters such as temperature, sample volume and overall methodology. It also includes the application of some unique procedures and approaches, and the addition of novel components such as detergents, ligands or other small molecules that may enhance nucleation or crystal development. Here, an attempt is made to provide guidance on how optimization might best be applied to crystal-growth problems, and what parameters and factors might most profitably be explored to accelerate and achieve success.

Indexed as

AnimalsCrystallizationCrystallography, X-RayHumansMacromolecular SubstancesOsmolar ConcentrationMacromolecular Substancesadditivescrystal growthnucleationpHprecipitantsproteinsstrategyX-ray diffraction

Identifiers

PMID25372810
PMCPMC4231845

What OpenQuestion holds

Textmetadata
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.