ArticleJournal of structural and functional genomics2014
Towards an integrative structural biology approach: combining Cryo-TEM, X-ray crystallography, and NMR.
Article in Journal of structural and functional genomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Research Progress on Sex Pheromone Receptors in Insects.Insects · 2026Review
- Temperature-Resolved Crystallography Reveals Rigid-Body Dominance over Local Flexibility in B‑Factors.ACS omega · 2025Article
- Cullin-Conciliated Regulation of Plant Immune Responses: Implications for Sustainable Crop Protection.Plants (Basel, Switzerland) · 2024Review
- Systematic computational strategies for identifying protein targets and lead discovery.RSC medicinal chemistry · 2024Review
- Lead-seq: transcriptome-wide structure probing in vivo using lead(II) ions.Nucleic acids research · 2020Article
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Reporting on the future of integrative structural biology ORAU workshop.Frontiers in bioscience (Landmark edition) · 2020Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- New Era of Studying RNA Secondary Structure and Its Influence on Gene Regulation in Plants.Frontiers in plant science · 2018Review
- Delineating distinct heme-scavenging and -binding functions of domains in MF6p/helminth defense molecule (HDM) proteins from parasitic flatworms.The Journal of biological chemistry · 2017Article
- Biochemical Methods To Investigate lncRNA and the Influence of lncRNA:Protein Complexes on Chromatin.Biochemistry · 2016Review
- X-ray structure determination using low-resolution electron microscopy maps for molecular replacement.Nature protocols · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryo-transmission electron microscopy (Cryo-TEM) and particularly single particle analysis is rapidly becoming the premier method for determining the three-dimensional structure of protein complexes, and viruses. In the last several years there have been dramatic technological improvements in Cryo-TEM, such as advancements in automation and use of improved detectors, as well as improved image processing techniques. While Cryo-TEM was once thought of as a low resolution structural technique, the method is currently capable of generating nearly atomic resolution structures on a routine basis. Moreover, the combination of Cryo-TEM and other methods such as X-ray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics modeling are allowing researchers to address scientific questions previously thought intractable. Future technological developments are widely believed to further enhance the method and it is not inconceivable that Cryo-TEM could become as routine as X-ray crystallography for protein structure determination.
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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.