Related references
Note: Only part of the references are listed.Structure of the Type VI Secretion System Contractile Sheath
Mikhail Kudryashev et al.
CELL (2015)
Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement
Frank DiMaio et al.
NATURE METHODS (2015)
De novo protein structure determination from near-atomic-resolution cryo-EM maps
Ray Yu-Ruei Wang et al.
NATURE METHODS (2015)
EMRinger: side chain directed model and map validation for 3D cryo-electron microscopy
Benjamin A. Barad et al.
NATURE METHODS (2015)
X-ray structure determination using low-resolution electron microscopy maps for molecular replacement
Ryan N. Jackson et al.
NATURE PROTOCOLS (2015)
2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
Melody G. Campbell et al.
ELIFE (2015)
Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
Alan Brown et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2015)
Initiation of Translation by Cricket Paralysis Virus IRES Requires Its Translocation in the Ribosome
Israel S. Fernandez et al.
CELL (2014)
Quantifying the local resolution of cryo-EMEM density maps
Alp Kucukelbir et al.
NATURE METHODS (2014)
Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
Alberto Bartesaghi et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
Relaxation of backbone bond geometry improves protein energy landscape modeling
Patrick Conway et al.
PROTEIN SCIENCE (2014)
Structure of the large ribosomal subunit from human mitochondria
Alan Brown et al.
SCIENCE (2014)
Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector
Matteo Allegretti et al.
ELIFE (2014)
Structure of the TRPV1 ion channel determined by electron cryo-microscopy
Maofu Liao et al.
NATURE (2013)
Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
Xueming Li et al.
NATURE METHODS (2013)
Cryo-EM model validation using independent map reconstructions
Frank DiMaio et al.
PROTEIN SCIENCE (2013)
Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
Xiao-chen Bai et al.
ELIFE (2013)
Use of knowledge-based restraints in phenix.refine to improve macromolecular refinement at low resolution
Jeffrey J. Headd et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2012)
Towards automated crystallographic structure refinement with phenix.refine
Pavel V. Afonine et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2012)
A Bayesian View on Cryo-EM Structure Determination
Sjors H. W. Scheres
JOURNAL OF MOLECULAR BIOLOGY (2012)
MolProbity: all-atom structure validation for macromolecular crystallography
Vincent B. Chen et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2010)
Features and development of Coot
P. Emsley et al.
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2010)
Neighbor-Dependent Ramachandran Probability Distributions of Amino Acids Developed from a Hierarchical Dirichlet Process Model
Daniel Ting et al.
PLOS COMPUTATIONAL BIOLOGY (2010)
X-ray structure determination at low resolution
Axel T. Brunger et al.
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2009)
Oxidative challenges sensitize the capsaicin receptor by covalent cysteine modification
Huai-hu Chuang et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Accurate structural correlations from maximum likelihood superpositions
Douglas L. Theobald et al.
PLOS COMPUTATIONAL BIOLOGY (2008)
Considerations for the refinement of low-resolution crystal structures
Byron DeLaBarre et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2006)
Share Paper
