ArticleActa crystallographica. Section D, Biological crystallography2010
Joint X-ray and neutron refinement with phenix.refine.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.
What it found
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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.
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Who cites it
180 citing papers in PubMed, 288 citations in OpenAlex.
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- Terminal alkyne formation by a pyridoxal phosphate-dependent enzyme.Nature chemical biology · 2026Article
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 2025Article
- Neutron crystallography of the covalent intermediate of β-glucosidase reveals remodeling of the catalytic center.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- ATP hydrolysis-driven structural transitions within the Saccharomyces cerevisiae Rad51 and Dmc1 nucleoprotein filaments.The Journal of biological chemistry · 2025Article
- Thermotolerant class A acid phosphatase active across broad pH range and diverse substrates.Protein science : a publication of the Protein Society · 2025Article
- Molecular mechanism of potently neutralizing human monoclonal antibodies against severe fever with thrombocytopenia virus infection.Journal of virology · 2025Article
- Characterization of a consensus-designedmBio · 2025Article
- Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination.bioRxiv : the preprint server for biology · 2025Article
- ATP hydrolysis-driven structural transitions within thebioRxiv : the preprint server for biology · 2025Article
- Bacterial sensor evolved by decreasing complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Structural basis for Mis18 complex assembly and its implications for centromere maintenance.EMBO reports · 2024Article
- Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria.Nature communications · 2024Article
- Modular binder technology by NGS-aided, high-resolution selection in yeast of designed armadillo modules.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural determination and kinetic analysis of the transketolase from Vibrio vulnificus reveal unexpected cooperative behavior.Protein science : a publication of the Protein Society · 2024Article
120 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Approximately 85% of the structures deposited in the Protein Data Bank have been solved using X-ray crystallography, making it the leading method for three-dimensional structure determination of macromolecules. One of the limitations of the method is that the typical data quality (resolution) does not allow the direct determination of H-atom positions. Most hydrogen positions can be inferred from the positions of other atoms and therefore can be readily included into the structure model as a priori knowledge. However, this may not be the case in biologically active sites of macromolecules, where the presence and position of hydrogen is crucial to the enzymatic mechanism. This makes the application of neutron crystallography in biology particularly important, as H atoms can be clearly located in experimental neutron scattering density maps. Without exception, when a neutron structure is determined the corresponding X-ray structure is also known, making it possible to derive the complete structure using both data sets. Here, the implementation of crystallographic structure-refinement procedures that include both X-ray and neutron data (separate or jointly) in the PHENIX system is described.
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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.