ArticleJournal of applied crystallography2017
Berkeley Screen: a set of 96 solutions for general macromolecular crystallization.
Article in Journal of applied crystallography, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 27 citations in OpenAlex.
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- The Crystal Structure of Human Transport and Golgi Organization 2 Homolog (TANGO2) Protein Reveals an αββα-Fold Arrangement.Proteins · 2026Article
- A highly active Burkholderia polyketoacyl-CoA thiolase for production of triacetic acid lactone.Nature communications · 2025Article
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Rational Exploration of 2,4-Diaminopyrimidines as DHFR Inhibitors Active againstJournal of medicinal chemistry · 2024Article
- Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates.Nature communications · 2024Article
- The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits.Scientific reports · 2024Article
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- Crystal structures of NAD(P)H nitroreductases from Klebsiella pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structural and biochemical insight into a modular β-1,4-galactan synthase in plants.Nature plants · 2023Article
- Structural plasticity enables evolution and innovation of RuBisCO assemblies.Science advances · 2022Article
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- Novel bacterial clade reveals origin of form I Rubisco.Nature plants · 2020Article
- Engineering glycoside hydrolase stability by the introduction of zinc binding.Acta crystallographica. Section D, Structural biology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using statistical analysis of the Biological Macromolecular Crystallization Database, combined with previous knowledge about crystallization reagents, a crystallization screen called the Berkeley Screen has been created. Correlating crystallization conditions and high-resolution protein structures, it is possible to better understand the influence that a particular solution has on protein crystal formation. Ions and small molecules such as buffers and precipitants used in crystallization experiments were identified in electron density maps, highlighting the role of these chemicals in protein crystal packing. The Berkeley Screen has been extensively used to crystallize target proteins from the Joint BioEnergy Institute and the Collaborative Crystallography program at the Berkeley Center for Structural Biology, contributing to several Protein Data Bank entries and related publications. The Berkeley Screen provides the crystallographic community with an efficient set of solutions for general macromolecular crystallization trials, offering a valuable alternative to the existing commercially available screens.
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