ArticleActa crystallographica. Section F, Structural biology communications2025
Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Scotty: lattice coincidences for macromolecular crystallographic phasing.Acta crystallographica. Section D, Structural biology · 2026Article
- Cryo-EM reveals ArnA contamination during purification of a ciliary protein complex.Acta crystallographica. Section D, Structural biology · 2026Article
- Bacterial β-carbonic anhydrases: a six-step prioritization framework for antibacterial target validation.Archives of microbiology · 2026Review
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Abstract
X-ray crystallography remains the dominant method of determining the three-dimensional structure of proteins. Nevertheless, this resource-intensive process may be hindered by the unintended crystallization of contaminant proteins from the expression source. Here, the serendipitous discovery of two novel crystal forms and one new, high-resolution structure of carbonic anhydrase 2 (CA2) from Escherichia coli that arose during a crystallization campaign for an unrelated target is reported. By comparing unit-cell parameters with those in the PDB, contaminants such as CA2 can be identified, preventing futile molecular-replacement attempts. Crystallographers can use these new lattice parameters to diagnose CA2 contamination in similar experiments.
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