Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
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David Eisenberg | Tamir Gonen | Michael R. Sawaya | Johan Hattne | Duilio Cascio | Dan Shi | Guillermo Calero | D. Eisenberg | A. Hinck | José A. Rodríguez | M. Sawaya | T. Gonen | D. Shi | M. J. de la Cruz | C. Hinck | D. Cascio | S. Kim | J. Hattne | P. Seidler | G. Calero | M. Jason de la Cruz | Paul Seidler | Jose Rodriguez | Francis E. Reyes | Simon C. Weiss | Sun Kyung Kim | Cynthia S. Hinck | Andrew P. Hinck | F. Reyes | S. Weiss | Sun Kyung Kim | Dan Shi | Francis E. Reyes | Sun Kyung Kim
[1] Randy J. Read,et al. Evolving Methods for Macromolecular Crystallography , 2007 .
[2] T. Gonen,et al. Structure of catalase determined by MicroED , 2014, eLife.
[3] Philip R. Evans,et al. How good are my data and what is the resolution? , 2013, Acta crystallographica. Section D, Biological crystallography.
[4] D. Eisenberg,et al. Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED , 2016, Proceedings of the National Academy of Sciences.
[5] A. Brunger. Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.
[6] C. Nave. A description of imperfections in protein crystals. , 1998, Acta crystallographica. Section D, Biological crystallography.
[7] R. Henderson. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules , 1995, Quarterly Reviews of Biophysics.
[8] Tamir Gonen,et al. MicroED data collection and processing , 2015, Acta crystallographica. Section A, Foundations and advances.
[9] Troy C. Krzysiak,et al. Transmission electron microscopy for the evaluation and optimization of crystal growth. , 2016, Acta crystallographica. Section D, Structural biology.
[10] A. Hinck,et al. Assembly of TβRI: TβRII:TGFβ ternary complex in vitro with receptor extracellular domains is cooperative and isoform-dependent , 2005 .
[11] T. Gonen,et al. Micro- and nanocrystal preparation for MicroED and XFEL serial crystallography by fragmentation of imperfect crystals , 2017 .
[12] K. Harata,et al. Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement. , 2006, Acta crystallographica. Section D, Biological crystallography.
[13] W. Delano. The PyMOL Molecular Graphics System , 2002 .
[14] Randy J. Read,et al. Overview of the CCP4 suite and current developments , 2011, Acta crystallographica. Section D, Biological crystallography.
[15] R E Hubbard,et al. Locating interaction sites on proteins: The crystal structure of thermolysin soaked in 2% to 100% isopropanol , 1999, Proteins.
[16] Ilme Schlichting,et al. Serial femtosecond crystallography: the first five years , 2015, IUCrJ.
[17] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[18] S. Harrison,et al. Lipid–protein interactions in double-layered two-dimensional AQP0 crystals , 2005, Nature.
[19] P. Zwart,et al. Towards automated crystallographic structure refinement with phenix.refine , 2012, Acta crystallographica. Section D, Biological crystallography.
[20] Sébastien Boutet,et al. Nanoflow electrospinning serial femtosecond crystallography. , 2012, Acta crystallographica. Section D, Biological crystallography.
[21] T. Gonen,et al. The collection of MicroED data for macromolecular crystallography , 2016, Nature Protocols.
[22] Garth J. Williams,et al. Structural studies of P-type ATPase–ligand complexes using an X-ray free-electron laser , 2015, IUCrJ.
[23] C. Darwin. XCII. The reflexion of X-rays from imperfect crystals , 1922 .
[24] Concerning the detection of X-ray interferences , 2018 .
[25] Tamir Gonen,et al. High-resolution structure determination by continuous rotation data collection in MicroED , 2014, Nature Methods.
[26] G. Sheldrick. SHELXT – Integrated space-group and crystal-structure determination , 2015, Acta crystallographica. Section A, Foundations and advances.
[27] Owen Johnson,et al. iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM , 2011, Acta crystallographica. Section D, Biological crystallography.
[28] Manfred Burghammer,et al. Small is beautiful: protein micro-crystallography , 1998, Nature Structural Biology.
[29] Koji Yonekura,et al. Electron crystallography of ultrathin 3D protein crystals: Atomic model with charges , 2015, Proceedings of the National Academy of Sciences.
[30] Uwe Weierstall,et al. Liquid sample delivery techniques for serial femtosecond crystallography , 2014, Philosophical Transactions of the Royal Society B: Biological Sciences.
[31] Tamir Gonen,et al. Three-dimensional electron crystallography of protein microcrystals , 2013, eLife.
[32] Nicholas K. Sauter,et al. Structure of the toxic core of α-synuclein from invisible crystals , 2015, Nature.
[33] G. Langlet,et al. International Tables for Crystallography , 2002 .
[34] A. Vagin,et al. MOLREP: an Automated Program for Molecular Replacement , 1997 .
[35] Oleg V. Tsodikov,et al. Data publication with the structural biology data grid supports live analysis , 2016, Nature Communications.
[36] T. Gonen,et al. Modeling truncated pixel values of faint reflections in MicroED images1 , 2016, Journal of applied crystallography.