ArticleActa crystallographica. Section D, Structural biology2021
Cryo-EM single-particle structure refinement and map calculation using Servalcat.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 213 papers.
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213 citing papers in PubMed.
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- Sequence-dependent binding modes of INO80 control +1 nucleosome positioning.bioRxiv : the preprint server for biology · 2026Article
- A ubiquitin chain-feeding mechanism for BRCA1-A.Nature communications · 2026Article
- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- 23S rRNA modifications stimulate catalytic activity and prevent the formation of alternative structures.Nucleic acids research · 2026Article
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- ESCRT-III assembles around mis-segregated DNA to protect genome stability.Nature structural & molecular biology · 2026Article
- Core-sheath coupling controls flagellar curvature and motility in Leptospira.Nature communications · 2026Article
- Supramolecular nanofiber stabilization of microdroplets enables ultra-sensitive virus infection analysis.Nature communications · 2026Article
153 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
In 2020, cryo-EM single-particle analysis achieved true atomic resolution thanks to technological developments in hardware and software. The number of high-resolution reconstructions continues to grow, increasing the importance of the accurate determination of atomic coordinates. Here, a new Python package and program called Servalcat is presented that is designed to facilitate atomic model refinement. Servalcat implements a refinement pipeline using the program REFMAC5 from the CCP4 package. After the refinement, Servalcat calculates a weighted F
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