ArticleActa crystallographica. Section D, Structural biology2024
Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.
Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.Acta crystallographica. Section D, Structural biology · 2026Article
- Pinpointing Protein Crystal Structures over a Broad Temperature Range Using Hydrophobic Protection.ACS omega · 2026Article
- An integrated experimental and computational pipeline for crystallographic fragment screening of membrane protein in the lipid cubic phase.Communications chemistry · 2026Article
- Room-temperature X-ray fragment screening with serial crystallography.Nature communications · 2025Article
- Temperature-Resolved Crystallography Reveals Rigid-Body Dominance over Local Flexibility in B‑Factors.ACS omega · 2025Article
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Advances in structural biology have relied heavily on synchrotron cryo-crystallography and cryogenic electron microscopy to elucidate biological processes and for drug discovery. However, disparities between cryogenic and room-temperature (RT) crystal structures pose challenges. Here, Cryo2RT, a high-throughput RT data-collection method from cryo-cooled crystals that leverages the cryo-crystallography workflow, is introduced. Tested on endothiapepsin crystals with four soaked fragments, thaumatin and SARS-CoV-2 3CL
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