The Resolution Revolution

By W. Kühlbrandt. 2014

1,123 citations recorded by the source corpus.

Subfields: Molecular Biology, Structural Biology

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Citations in the corpus

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, methodology): “While validation methods in crystallography have had decades to mature, cryo-EM has only recently evolved into a routine technique for near-atomic resolution models (Kühlbrandt, 2014).”
New tools for automated high-resolution cryo-EM structure determination in RELION-3 (2018, background): “Together, they led to what was termed the ’resolution revolution’ in cryo-EM structure determination ( Kuhlbrandt, 2014 ).”
Recent developments in the CCP-EM software suite (2017, background): “This focus partly reflects our historical links to the macromolecular crystallography community, but is also timely given the recent ‘resolution revolution’ (Kühlbrandt, 2014).”
Automated map sharpening by maximization of detail and connectivity (2018, methodology): “Current methods for single-particle reconstruction of cryo-EM maps are capable of yielding maps with resolution often better than 4.5 Å and sometimes as high as 2 Å or better (c.f., Kuhlbrandt, 2014; Baldwin et al., 2018).”
New tools for the analysis and validation of cryo-EM maps and atomic models (2018, background): “Cryo-EM is just entering the era of routine use at near-atomic resolution (Kuhlbrandt, 2014) with atomic models built de novo based on experimental maps.”
Mechanistic diversity in ATP-binding cassette (ABC) transporters (2016, background): “However, given the recent resolution revolution in single particle cryo-EM 85 , even single ABC transporters may soon be studied at high resolution without the need to grow three-dimensional crystals.”
Single-Particle Cryo-EM at Crystallographic Resolution. (2015, background): “Here, I will briefly summarize the recent technological advancements and how they enabled a ‘‘resolution revolution’’ (Kühlbrandt, 2014).”
New tools for automated cryo-EM single-particle analysis in RELION-4.0 (2021, methodology): “The cryo-EM resolution revolution [11] further accelerated the focus on user-oriented software developments, with new software packages like SPHIRE [12], cisTEM [13] and the commercial cryoSPARC [14] implementing robust and easy-to-use pipelines for”
Solving the scalability issue in quantum-based refinement: Q|R#1. (2017, methodology): “Introduction Crystallography is the dominant method for obtaining the atomic structure of a protein; however, it has recently been reported that a cryo-EM revolution is under way (Egelman, 2016; Kühlbrandt, 2014; Callaway, 2015).”
ScanNet: an interpretable geometric deep learning model for structure-based protein binding site prediction (2021, methodology): “To this end, the NAM learns (1) a diffusion kernel on the residue–residue graph (the algebraic edges) and (2) importance coefficients for each node.”
BioEM: GPU-accelerated computing of Bayesian inference of electron microscopy images (2016, methodology): “Bayesian analysis methods, such as Relion [14, 15], have been enormously successful in EM, contributing much to the resolution revolution [2].”
Assessment of protein assembly prediction in CASP13 (2019, neutral): “8 Å in 2018) [10][11].”