ArticleActa crystallographica. Section F, Structural biology communications2014
A drunken search in crystallization space.
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 29 papers.
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.
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.
Who cites it
29 citing papers in PubMed.
- Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026Article
- Influence of heme and pH on the oligomeric states of Brucella melitensis bacterioferritin.Acta crystallographica. Section D, Structural biology · 2026Article
- Structural characterisation of nucleotide sugar short-chain dehydrogenases/reductases from the thermophilic pseudomurein-containing methanogen Methanothermobacter thermautotrophicus ΔH.The FEBS journal · 2026Article
- Streptococcus pneumoniae HtrA is a dynamic and monomeric virulence factor capable of forming larger oligomeric complexes.Protein science : a publication of the Protein Society · 2026Article
- The Starting Point for Biomolecular Crystallisation.Advances in biochemical engineering/biotechnology · 2026Review
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identifying and controlling inactive and active conformations of a serine protease.Science advances · 2025Article
- Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting.Frontiers in plant science · 2024Article
- 20 years of crystal hits: progress and promise in ultrahigh-throughput crystallization screening.Acta crystallographica. Section D, Structural biology · 2023Article
- Not getting in too deep: A practical deep learning approach to routine crystallisation image classification.PloS one · 2023Article
- Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach.Protein science : a publication of the Protein Society · 2022Article
- A new crystal form of GABARAPL2.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Article
- FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.The EMBO journal · 2020Article
- Crystal structures of human ENPP1 in apo and bound forms.Acta crystallographica. Section D, Structural biology · 2020Article
- A Searchable Database of Crystallization Cocktails in the PDB: Analyzing the Chemical Condition Space.Patterns (New York, N.Y.) · 2020Article
- Structure of Sonic Hedgehog protein in complex with zinc(II) and magnesium(II) reveals ion-coordination plasticity relevant to peptide drug design.Acta crystallographica. Section D, Structural biology · 2019Article
- BLASTing away preconceptions in crystallization trials.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Iterative screen optimization maximizes the efficiency of macromolecular crystallization.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Can the propensity of protein crystallization be increased by using systematic screening with metals?Protein science : a publication of the Protein Society · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The REMARK280 field of the Protein Data Bank is the richest open source of successful crystallization information. The REMARK280 field is optional and currently uncurated, so significant effort needs to be applied to extract reliable data. There are well over 15 000 crystallization conditions available commercially from 12 different vendors. After putting the PDB crystallization information and the commercial cocktail data into a consistent format, these data are used to extract information about the overlap between the two sets of crystallization conditions. An estimation is made as to which commercially available conditions are most appropriate for producing well diffracting crystals by looking at which commercial conditions are found unchanged (or almost unchanged) in the PDB. Further analyses include which commercial kits are the most appropriate for shotgun or more traditional approaches to crystallization screening. This analysis suggests that almost 40% of the crystallization conditions found currently in the PDB are identical or very similar to a commercial condition.
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Registered trials
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.