This Month |
Featured
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Article |
Aromatic 19F-13C TROSY: a background-free approach to probe biomolecular structure, function, and dynamics
The development of 19F-13C TROSY provides a new avenue for the collection of high-sensitivity, background-free information about the structure and dynamics of challenging biomolecular systems by NMR spectroscopy.
- Andras Boeszoermenyi
- , Sandeep Chhabra
- & Haribabu Arthanari
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Perspective |
An online resource for GPCR structure determination and analysis
An interactive online resource integrated in the GPCRdb hub presents tools to design GPCR constructs and determine appropriate experimental conditions for structural studies by crystallography and cryo-EM.
- Christian Munk
- , Eshita Mutt
- & David E. Gloriam
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Editorial |
Challenges for cryo-EM
Two community challenges assess the correctness of cryo-EM structures; future challenges should help determine the most appropriate structure validation methods.
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Article |
A particle-filter framework for robust cryo-EM 3D reconstruction
A particle-filter algorithm for single-particle cryo-electron microscopy, implemented in a tool called THUNDER, provides high-dimensional parameter estimation, improving the obtainable resolution for several protein structures.
- Mingxu Hu
- , Hongkun Yu
- & Xueming Li
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Research Highlight |
High-speed protein crystallography
The European XFEL produces its first protein structures.
- Allison Doerr
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Brief Communication |
A fully automatic method yielding initial models from high-resolution cryo-electron microscopy maps
A fully automated method for modeling protein and protein–RNA complex structure from cryo-EM data, requiring minimal user intervention, is described.
- Thomas C. Terwilliger
- , Paul D. Adams
- & Oleg V. Sobolev
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Brief Communication |
The hit-and-return system enables efficient time-resolved serial synchrotron crystallography
A data-collection strategy using a fixed-target crystallography chip allows time-resolved serial synchrotron crystallography experiments to determine enzyme intermediate structures with time resolutions of milliseconds to seconds.
- Eike C. Schulz
- , Pedram Mehrabi
- & R. J. Dwayne Miller
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Article |
De novo computational RNA modeling into cryo-EM maps of large ribonucleoprotein complexes
DRRAFTER, a method for RNA modeling into cryo-EM maps, generates accurate models for diverse RNA–protein complexes.
- Kalli Kappel
- , Shiheng Liu
- & Rhiju Das
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Article |
emClarity: software for high-resolution cryo-electron tomography and subtomogram averaging
A software tool, emClarity, implements several improvements in cryo-electron tomography image-processing algorithms to achieve sub-nanometer resolution for diverse macromolecular structures.
- Benjamin A. Himes
- & Peijun Zhang
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News & Views |
A detector for the sources
A new detector built for X-ray free-electron lasers provides unprecedented speed and accuracy for macromolecular crystallography at synchrotron radiation facilities—and finally allows crystallographers to harness the full capabilities of those sources.
- Henry N. Chapman
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This Month |
Bridget Carragher
Speeding up spot-to-plunge in cryo-EM and how to keep a lab talking.
- Vivien Marx
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Article |
Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector
A charge-integrating pixel-array detector called JUNGFRAU enables the collection of highly accurate X-ray crystallography data at synchrotron sources at unprecedented speeds.
- Filip Leonarski
- , Sophie Redford
- & Meitian Wang
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Brief Communication |
Multicolor single-particle reconstruction of protein complexes
A computational and analytical framework enables multicolor 3D particle reconstruction of protein complexes from 2D images. The authors demonstrate the power of the approach by reconstructing native proteins within the human centriole.
- Christian Sieben
- , Niccolò Banterle
- & Suliana Manley
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Brief Communication |
Reducing effects of particle adsorption to the air–water interface in cryo-EM
Reducing the length of time that protein particles spend on a sample grid prior to freezing mitigates deleterious effects caused by particle adsorption to the air–water interface in single-particle cryo-EM.
- Alex J. Noble
- , Hui Wei
- & Bridget Carragher
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Brief Communication |
COMRADES determines in vivo RNA structures and interactions
In vivo probing of RNA structures with COMRADES yields insight into RNA folding of the ZIKA virus genome and its interaction with host RNAs.
- Omer Ziv
- , Marta M. Gabryelska
- & Eric A. Miska
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Research Highlight |
A path to predict RNA tertiary structures
A high-throughput platform allows biophysical measurements to probe RNA tertiary folding.
- Lei Tang
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Research Highlight |
Taking inventory with shotgun EM
The combination of single-particle electron microscopy and mass spectrometry shows potential for surveys of both the structure and the identity of protein complexes in the cell.
- Allison Doerr
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Analysis
| Open AccessPrecision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
A multi-laboratory study finds that single-molecule FRET is a reproducible and reliable approach for determining accurate distances in dye-labeled DNA duplexes.
- Björn Hellenkamp
- , Sonja Schmid
- & Thorsten Hugel
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Research Highlight |
A home for integrative structural models
PDB-Dev hosts integrative structural models of biomolecular assemblies solved by hybrid methods.
- Allison Doerr
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Tools in Brief |
cisTEM software for cryo-EM
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Tools in Brief |
Local resolution of cryo-EM maps with MonoRes
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Tools in Brief |
The Protein Contacts Atlas
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Methods in Brief |
Light-based RNA structure probing
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Brief Communication |
Ab initio electron density determination directly from solution scattering data
An iterative structure factor retrieval algorithm allows electron densities to be directly calculated from solution scattering data, avoiding assumptions that limit modeling algorithms.
- Thomas D Grant
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Methods in Brief |
Improving the efficiency of cryo-EM
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Correspondence |
LiteMol suite: interactive web-based visualization of large-scale macromolecular structure data
- David Sehnal
- , Mandar Deshpande
- & Jaroslav Koča
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Correspondence |
Accessible virtual reality of biomolecular structural models using the Autodesk Molecule Viewer
- Aidin R Balo
- , Merry Wang
- & Oliver P Ernst
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Brief Communication |
Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV
Cryo-EM-based structure determination of macromolecular complexes at near-atomic resolution is possible using a mid-range 200-keV transmission electron microscope instrument.
- Mark A Herzik Jr
- , Mengyu Wu
- & Gabriel C Lander
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Article |
Conformational landscape of a virus by single-particle X-ray scattering
A 9-nm-resolution structure of PR772 virus and a movie of its continuous conformational changes are determined from single-particle X-ray scattering data.
- Ahmad Hosseinizadeh
- , Ghoncheh Mashayekhi
- & Abbas Ourmazd
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Article |
M3: an integrative framework for structure determination of molecular machines
Structure determination of large molecular machines is facilitated by M3, a broadly applicable and user-friendly modeling method that takes diverse structural and biochemical data as inputs.
- Ezgi Karaca
- , João P G L M Rodrigues
- & Teresa Carlomagno
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Brief Communication |
Addressing preferred specimen orientation in single-particle cryo-EM through tilting
The preferred specimen orientation problem limits accuracy and resolution in structure determination by cryo-EM. Collecting data at defined sample tilts yielded near-atomic-resolution structures for the influenza hemagglutinin trimer and ribosomal biogenesis intermediates.
- Yong Zi Tan
- , Philip R Baldwin
- & Dmitry Lyumkis
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Methods in Brief |
Single-protein detection by cryo-EM
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Brief Communication |
RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps
RosettaES, an algorithm that uses a fragment-based sampling strategy, improves macromolecular structure modeling from cryo-EM data at 3–5-Å resolution.
- Brandon Frenz
- , Alexandra C Walls
- & Frank DiMaio
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Article |
High-speed fixed-target serial virus crystallography
A new sample-delivery method for serial X-ray crystallography exploits the full repetition rate of the X-ray free-electron laser at the LCLS facility, thus enabling efficient, high-speed data collection to solve the three-dimensional structures of viruses.
- Philip Roedig
- , Helen M Ginn
- & Alke Meents
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Tools in Brief |
GPCR function insights by cryo-EM
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Methods in Brief |
Solution-state 13C NMR gets a boost
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Brief Communication |
Structural modeling of protein–RNA complexes using crosslinking of segmentally isotope-labeled RNA and MS/MS
A mass spectrometry–based method to pinpoint UV-induced crosslinks in ribonucleoprotein complexes at protein residue and RNA nucleotide resolution provides key structural information for integrative modeling.
- Georg Dorn
- , Alexander Leitner
- & Frédéric H-T Allain
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Correspondence |
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions.
- Shawn Q Zheng
- , Eugene Palovcak
- & David A Agard
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Article |
Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers
A robust acoustic droplet ejection–drop-on-tape method delivers samples to an X-ray free-electron laser source for combined serial femtosecond crystallography and X-ray emission spectroscopy analysis, providing detailed insights into macromolecular reaction dynamics.
- Franklin D Fuller
- , Sheraz Gul
- & Junko Yano
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Brief Communication |
Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED
Fragmentation of large, imperfect crystals into nanocrystals by sonication, vortexing, or vigorous pipetting facilitates atomic-resolution analysis by the cryo-EM method MicroED.
- M Jason de la Cruz
- , Johan Hattne
- & Tamir Gonen
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Article |
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
A software tool, cryoSPARC, addresses the speed bottleneck in cryo-EM image processing, enabling automated macromolecular structure determination in hours on a desktop computer without requiring a starting model.
- Ali Punjani
- , John L Rubinstein
- & Marcus A Brubaker
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Methods in Brief |
Probing protein mechanics with an electric field
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Brief Communication |
High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles
Instrumental modifications enable native mass spectrometry analysis with unprecedented mass resolution, especially at high mass-to-charge ratios, as illustrated through the analysis of intact ribosome particles.
- Michiel van de Waterbeemd
- , Kyle L Fort
- & Albert J R Heck
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Brief Communication |
Cryogenic optical localization provides 3D protein structure data with Angstrom resolution
The positions of fluorophores can be localized in single proteins with Angstrom-scale resolution using Cryogenic Optical Localization in 3D (COLD), a complementary approach to traditional structural biology techniques.
- Siegfried Weisenburger
- , Daniel Boening
- & Vahid Sandoghdar
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Method to Watch |
Cryo-electron tomography
Cryo-electron tomography may facilitate in situ structural biology on a proteomic scale.
- Allison Doerr
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Research Highlights |
Colorful electron microscopy
A multicolor approach specifically labels multiple targets in electron microscopy images.
- Rita Strack
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Research Highlights |
Blend-and-shoot crystallography
A rapid mix-and-inject serial femtosecond crystallography approach enables structure determination of ligand-binding intermediates.
- Allison Doerr