FREALIGN: high-resolution refinement of single particle structures.
By N. Grigorieff. Journal of Structural Biology, 2007
536 citations recorded by the source corpus.
Subfields: Molecular Biology, Structural Biology, Surfaces, Coatings and Films
View Paper: https://www.semanticscholar.org/paper/55257ac01aed277506a3e55d6c9a7ec4557c3086
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In Molecular Biology
- Sjors H. W. Scheres
- David J. Fleet
- Ali Punjani
- Kai Zhang
- G. Murshudov
- N. Grigorieff
- Dari Kimanius
- Erik Lindahl
In Structural Biology
- Sjors H. W. Scheres
- David J. Fleet
- Ali Punjani
- Kai Zhang
- Takanori Nakane
- Dari Kimanius
- Erik Lindahl
- G. Murshudov
In Surfaces, Coatings and Films
- Sjors H. W. Scheres
- David J. Fleet
- Ali Punjani
- Kai Zhang
- Dari Kimanius
- Takanori Nakane
- G. Murshudov
- Erik Lindahl
Citations in the corpus
- High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy (2013, methodology): “Stacks of particles were picked by hand using Ximdisp [50], CTF estimated using CTFFIND3 [51], boxed particle densities floated and normalised using BOXIMAGE [52], and 3D maps calculated using Frealign [9], Relion [10], Xmipp [53,54] and a new program still under development by McMullan (unpublished”
- Gctf: Real-time CTF determination and correction (2015, methodology): “For typical usage (box size 512 pixels and search step 500Å), Gctf can process more than 1000 micrographs in the time CTFFIND3 requires to process one.”
- Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2 (2016, unknown): “, 2007), frealign (Grigorieff, 2007), xmipp (Scheres et al.”
- Current approaches for the fitting and refinement of atomic models into cryo-EM maps using CCP-EM (2018, methodology): “Reconstructions are typically performed in Fourier space using the projection-slice theorem, as for example in RELION (Scheres, 2012) and Frealign (Grigorieff, 2007), before the reconstructed maps are subsequently calculated in real space.”
- Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction (2019, methodology): “In the standard cryo-EM 3D reconstruction problem set up [12, 22, 26], a generative model describes the formation of images of a target protein in an electron microscope.”
- cisTEM: User-friendly software for single-particle image processing (2017, methodology): “17 Score-based weighting In previous versions of Frealign, resolution-dependent weighting was 344 applied to the particle images during reconstruction (the Frealign parameter was called “PBC”, 345 (Grigorieff, 2007)).”
- A Bayesian View on Cryo-EM Structure Determination (2012, methodology): “XMIPP uses a constant for the SNR term in the Wiener filter and sets its value in the same way as FREALIGN does.(26) As also mentioned above, a single value is, however, inadequate to describe the intrinsic 3D behavior of the SNR in Fourier space.”
- High resolution microtubule structures reveal the structural transitions in αβ–tubulin upon GTP hydrolysis (2014, methodology): “A final refinement of the alignment parameters was performed only for the 14 pf MT particles using FREALIGN (Grigorieff, 2007), with a modified script that incorporated the symmetrization and MT seam regeneration after each round.”
- A Primer to Single-Particle Cryo-Electron Microscopy (2015, unknown): “, 2013) using RELION (Scheres, 2012) and FREALIGN (Grigorieff, 2007; Lyumkis et al., 2013) produces virtually identical features in the well-defined density regions within the transmembrane domain (Figure 4A-D).”
- 3D Variability Analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM (2020, methodology): “Under the standard cryo-EM image formation model (Frank, 2007; Grigorieff, 2007; Punjani et al., 2017; Scheres, 2012a), a 2D particle image, Xi, is a corrupted projection of the target 3D density V from an unobserved pose φi, plus additive noise, η.”