ArticleProtein science : a publication of the Protein Society2016
Protein purification and crystallization artifacts: The tale usually not told.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed.
- Sulfate-compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Bacterial β-carbonic anhydrases: a six-step prioritization framework for antibacterial target validation.Archives of microbiology · 2026Review
- A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025Article
- Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Filling in missing puzzle pieces in protein structural biology with cross-linking mass spectrometry.QRB discovery · 2025Review
- Ligand-based pharmacophore modeling and machine learning for the discovery of potent aurora A kinase inhibitory leads of novel chemotypes.Molecular diversity · 2024Article
- Ice Isn't the Only Crystal in Town: Structure Determination of Ice-Binding Proteins via X-Ray Crystallography.Methods in molecular biology (Clifton, N.J.) · 2024Article
- DoubleHelix: nucleic acid sequence identification, assignment and validation tool for cryo-EM and crystal structure models.Nucleic acids research · 2023Article
- PurificationDB: database of purification conditions for proteins.Database : the journal of biological databases and curation · 2023Article
- CMM-An enhanced platform for interactive validation of metal binding sites.Protein science : a publication of the Protein Society · 2023Article
- Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo.Nature communications · 2022Article
- Identification, structure determination and analysis of Mycobacterium smegmatis acyl-carrier protein synthase (AcpS) crystallized serendipitously.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Article
- Article
- Analysis of Two SusE-Like Enzymes FromFrontiers in microbiology · 2021Article
- Crystal structure of the Escherichia coli transcription termination factor Rho.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Contamination or serendipity - doing the wrong thing by chance.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Detecting the nature and solving the crystal structure of a contaminant protein from an opportunistic pathogen.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu.Nature methods · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
The misidentification of a protein sample, or contamination of a sample with the wrong protein, may be a potential reason for the non-reproducibility of experiments. This problem may occur in the process of heterologous overexpression and purification of recombinant proteins, as well as purification of proteins from natural sources. If the contaminated or misidentified sample is used for crystallization, in many cases the problem may not be detected until structures are determined. In the case of functional studies, the problem may not be detected for years. Here several procedures that can be successfully used for the identification of crystallized protein contaminants, including: (i) a lattice parameter search against known structures, (ii) sequence or fold identification from partially built models, and (iii) molecular replacement with common contaminants as search templates have been presented. A list of common contaminant structures to be used as alternative search models was provided. These methods were used to identify four cases of purification and crystallization artifacts. This report provides troubleshooting pointers for researchers facing difficulties in phasing or model building.
Indexed as
Identifiers
What OpenQuestion holds
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.