ArticleActa crystallographica. Section F, Structural biology communications2019
BLASTing away preconceptions in crystallization trials.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- The Starting Point for Biomolecular Crystallisation.Advances in biochemical engineering/biotechnology · 2026Review
- Using AlphaFold and Symmetrical Docking to Predict Protein-Protein Interactions for Exploring Potential Crystallization Conditions.Proteins · 2025Article
- Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025Article
- High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography.Journal of visualized experiments : JoVE · 2023Article
- Not getting in too deep: A practical deep learning approach to routine crystallisation image classification.PloS one · 2023Article
- IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition.Acta crystallographica. Section D, Structural biology · 2021Article
- A Searchable Database of Crystallization Cocktails in the PDB: Analyzing the Chemical Condition Space.Patterns (New York, N.Y.) · 2020Article
- Article
- A comparative anatomy of protein crystals: lessons from the automatic processing of 56 000 samples.IUCrJ · 2019Article
- Welcoming Janet Newman with a BLAST on crystallization strategy.Acta crystallographica. Section F, Structural biology communications · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystallization is in many cases a critical step for solving the three-dimensional structure of a protein molecule. Determining which set of chemicals to use in the initial screen is typically agnostic of the protein under investigation; however, crystallization efficiency could potentially be improved if this were not the case. Previous work has assumed that sequence similarity may provide useful information about appropriate crystallization cocktails; however, the authors are not aware of any quantitative verification of this assumption. This research investigates whether, given current information, one can detect any correlation between sequence similarity and crystallization cocktails. BLAST was used to quantitate the similarity between protein sequences in the Protein Data Bank, and this was compared with three estimations of the chemical similarities of the respective crystallization cocktails. No correlation was detected between proteins of similar (but not identical) sequence and their crystallization cocktails, suggesting that methods of determining screens based on this assumption are unlikely to result in screens that are better than those currently in use.
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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.