ArticleActa crystallographica. Section D, Structural biology2019
Coping with strong translational noncrystallographic symmetry and extreme anisotropy in molecular replacement with Phaser: human Rab27a.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 9 citations in OpenAlex.
- Improved protein binder design using β-pairing targeted RFdiffusion.Nature communications · 2026Article
- Likelihood-based signal and noise analysis for docking of models into cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2023Article
- Identification of the first structurally validated covalent ligands of the small GTPase RAB27A.RSC medicinal chemistry · 2022Article
- How do I get the most out of my protein sequence using bioinformatics tools?Acta crystallographica. Section D, Structural biology · 2021Article
- Introduction to molecular replacement: a time perspective.Acta crystallographica. Section D, Structural biology · 2021Review
- Detection of translational noncrystallographic symmetry in Patterson functions.Acta crystallographica. Section D, Structural biology · 2021Article
- Phasertng: directed acyclic graphs for crystallographic phasing.Acta crystallographica. Section D, Structural biology · 2021Article
- Measuring and using information gained by observing diffraction data.Acta crystallographica. Section D, Structural biology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Data pathologies caused by effects such as diffraction anisotropy and translational noncrystallographic symmetry (tNCS) can dramatically complicate the solution of the crystal structures of macromolecules. Such problems were encountered in determining the structure of a mutant form of Rab27a, a member of the Rab GTPases. Mutant Rab27a constructs that crystallize in the free form were designed for use in the discovery of drugs to reduce primary tumour invasiveness and metastasis. One construct, hRab27a
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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.