ReviewProtein science : a publication of the Protein Society2017
While the revolution will not be crystallized, biochemistry reigns supreme.
Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed.
- Cryo-EM Structure of Human ATAD2B Reveals a Hexameric Organization Contributes to ATPase Activity and Substrate Coordination.bioRxiv : the preprint server for biology · 2026Article
- Purifying recombinant proteins from Nicotiana benthamiana for structural studies.Nature protocols · 2026Review
- Breaking barriers: transitioning from X-ray crystallography to cryo-EM for structural studies.Acta crystallographica. Section D, Structural biology · 2026Article
- Breaking Barriers: Transitioning from X-ray Crystallography to Cryo-EM for Structural Studies of ATAD2B.bioRxiv : the preprint server for biology · 2025Article
- Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Multiparameter screen optimizes immunoprecipitation.BioTechniques · 2024Article
- Structural Insights into the Advances and Mechanistic Understanding of Human Dicer.Biochemistry · 2023Review
- Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM.Structure (London, England : 1993) · 2021Article
- Article
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- Methods for merging data sets in electron cryo-microscopy.Acta crystallographica. Section D, Structural biology · 2019Article
- Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit.International journal of molecular sciences · 2019Review
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Role of integrative structural biology in understanding transcriptional initiation.Methods (San Diego, Calif.) · 2019Review
- Challenges and opportunities in cryo-EM single-particle analysis.The Journal of biological chemistry · 2019Review
- Dawning of a new era in TRP channel structural biology by cryo-electron microscopy.Pflugers Archiv : European journal of physiology · 2018Review
- Article
- Cryo-EM: beyond the microscope.Current opinion in structural biology · 2017Review
- Structural and functional analyses of the spliceosome requires a multi-disciplinary approach.Methods (San Diego, Calif.) · 2017Article
- Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery.Acta crystallographica. Section F, Structural biology communications · 2017Review
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.
Funding
Abstract
Single-particle cryo-electron microscopy (EM) is currently gaining attention for the ability to calculate structures that reach sub-5 Å resolutions; however, the technique is more than just an alternative approach to X-ray crystallography. Molecular machines work via dynamic conformational changes, making structural flexibility the hallmark of function. While the dynamic regions in molecules are essential, they are also the most challenging to structurally characterize. Single-particle EM has the distinct advantage of being able to directly visualize purified molecules without the formation of ordered arrays of molecules locked into identical conformations. Additionally, structures determined using single-particle EM can span resolution ranges from very low- to atomic-levels (>30-1.8 Å), sometimes even in the same structure. The ability to accommodate various resolutions gives single-particle EM the unique capacity to structurally characterize dynamic regions of biological molecules, thereby contributing essential structural information needed for the development of molecular models that explain function. Further, many important molecular machines are intrinsically dynamic and compositionally heterogeneous. Structures of these complexes may never reach sub-5 Å resolutions due to this flexibility required for function. Thus, the biochemical quality of the sample, as well as, the calculation and interpretation of low- to mid-resolution cryo-EM structures (30-8 Å) remains critical for generating insights into the architecture of many challenging biological samples that cannot be visualized using alternative techniques.
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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.