Featured
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Brief Communication |
Deep-tissue SWIR imaging using rationally designed small red-shifted near-infrared fluorescent protein
miRFP718nano is a rationally designed small near-infrared fluorescent protein with an emission tail that extends into the short-wave infrared range for improved multiplexed and deep-tissue imaging applications.
- Olena S. Oliinyk
- , Chenshuo Ma
- & Vladislav V. Verkhusha
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Research Highlight |
Quantifying radiation damage
Bnet provides a measure of radiation damage suffered by protein crystals during X-ray crystallography.
- Arunima Singh
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Comment |
A new era of synchrotron-enabled macromolecular crystallography
The future of macromolecular crystallography includes new X-ray sources, enhanced remote-accessible capabilities and time-resolved methods to capture intermediate structures along reaction pathways.
- Aina E. Cohen
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Brief Communication |
Illumination guidelines for ultrafast pump–probe experiments by serial femtosecond crystallography
Theoretical and experimental guidelines to determine laser intensity for single-photon excitation in microcrystals for ultrafast pump–probe experiments by serial femtosecond crystallography.
- Marie Luise Grünbein
- , Miriam Stricker
- & Ilme Schlichting
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Article |
Time-resolved serial femtosecond crystallography at the European XFEL
European XFEL allows investigation of the picosecond time range in the photocycle of photoactive yellow protein.
- Suraj Pandey
- , Richard Bean
- & Marius Schmidt
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Brief Communication |
Liquid application method for time-resolved analyses by serial synchrotron crystallography
A rapid sample mixing approach enables time-resolved structural studies of enzymatic reactions using serial synchrotron crystallography.
- Pedram Mehrabi
- , Eike C. Schulz
- & R. J. Dwayne Miller
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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 |
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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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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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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Tools in Brief |
The Protein Contacts Atlas
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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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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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Methods in Brief |
Probing protein mechanics with an electric field
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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
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Article |
Multidomain structure and correlated dynamics determined by self-consistent FRET networks
A hybrid approach merges networks of time-correlated distances determined by single-molecule FRET to uncover local and global dynamics of the multidomain protein Hsp90 in solution at multiple timescales.
- Björn Hellenkamp
- , Philipp Wortmann
- & Thorsten Hugel
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Methods in Brief |
Laser ablation for growing protein crystals
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Tools in Brief |
Delivering crystals with sound
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Research Highlights |
Breaking the diffraction barrier
Researchers exploit crystal imperfections to solve protein structures at resolutions beyond the X-ray diffraction limit.
- Allison Doerr
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Method to Watch |
Protein structure through time
Advances in time-resolved crystallography make it possible to follow ever more rapid protein structural changes.
- Allison Doerr
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This Month |
Hasan DeMirci
The connection between snowboarding and getting more data from protein crystals.
- Vivien Marx
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Brief Communication |
Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II
A concentric-flow microfluidic electrokinetic sample injector enables efficient delivery of microcrystals in their mother liquor for serial femtosecond X-ray crystallography with minimal sample consumption.
- Raymond G Sierra
- , Cornelius Gati
- & Hasan DeMirci
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Tools in Brief |
A suite of oligomeric GFP variants
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Article |
Mutational interference mapping experiment (MIME) for studying RNA structure and function
Functionally important residues in a long RNA can be identified by mutational interference mapping experiment (MIME), a method which uses random mutagenesis of RNA followed by selection for function and high-throughput sequencing.
- Redmond P Smyth
- , Laurence Despons
- & Roland Marquet
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Article |
ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space
ProteoPlex optimizes buffer conditions for the isolation and purification of macromolecular complexes. The concurrent complex stabilization is beneficial for structure determination using X-ray crystallography or cryo-electron microscopy.
- Ashwin Chari
- , David Haselbach
- & Holger Stark
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Research Highlights |
Solving XFEL's image problem
Improved XFEL crystallography data processing methods enable structure determination from limited samples.
- Stéphane Larochelle
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Research Highlights |
XFELs probe protein dynamics
A new study shows that time-resolved serial femtosecond crystallography can reveal high-resolution intermediates of photoactive yellow protein.
- Rita Strack
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Method to Watch |
Structures from tiny crystals
Protein structures can be determined from microcrystals using X-ray and electron diffraction.
- Allison Doerr
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Brief Communication |
Macromolecular X-ray structure determination using weak, single-wavelength anomalous data
An improved analysis approach for single-wavelength anomalous diffraction (SAD)-based macromolecular X-ray structure determination expands the applicability of this phasing method for macromolecules with weak anomalous signals.
- Gábor Bunkóczi
- , Airlie J McCoy
- & Thomas C Terwilliger
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Brief Communication |
Fast native-SAD phasing for routine macromolecular structure determination
A native-SAD (single-wavelength anomalous diffraction) data collection strategy enables phasing using anomalous signal from a single native crystal, facilitating straightforward macromolecular X-ray structure determination.
- Tobias Weinert
- , Vincent Olieric
- & Meitian Wang
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Brief Communication |
Grease matrix as a versatile carrier of proteins for serial crystallography
Serial femtosecond crystallography experiments with diverse protein microcrystal suspensions are facilitated using a grease matrix as a carrier medium for sample injection.
- Michihiro Sugahara
- , Eiichi Mizohata
- & So Iwata
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Brief Communication |
Time-resolved crystallography using the Hadamard transform
A method based on the Hadamard transform is shown to enable time-resolved X-ray crystallography measurements of protein dynamics at standard synchrotron sources.
- Briony A Yorke
- , Godfrey S Beddard
- & Arwen R Pearson
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This Month |
Richard Neutze
Proteins 'breathe' in an ultrafast way that can be captured with XFELs.
- Vivien Marx
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Editorial |
A bittersweet celebration of crystallography
The Protein Structure Initiative will end next year; the aftershocks of this ending should be minimized for the benefit of the broader biology research community.
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Brief Communication |
Determination of damage-free crystal structure of an X-ray–sensitive protein using an XFEL
By combining the use of relatively large crystals and an X-ray free-electron laser, a radiation damage–free three-dimensional structure of a radiation-sensitive protein (bovine cytochrome oxidase) was solved at 1.9-Å resolution.
- Kunio Hirata
- , Kyoko Shinzawa-Itoh
- & Hideo Ago
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Brief Communication |
Accurate macromolecular structures using minimal measurements from X-ray free-electron lasers
A computational approach and software tool, cctbx.xfel, enables the determination of accurate macromolecular structure factors using a relatively small number of serial femtosecond crystallography diffraction snapshots.
- Johan Hattne
- , Nathaniel Echols
- & Nicholas K Sauter
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Research Highlights |
Making protein crystals fly
A new device for injecting membrane-protein microcrystals into the path of an X-ray free-electron laser beam improves the efficiency of serial femtosecond crystallography.
- Allison Doerr
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Methods in Brief |
A solution to the phasing problem
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Brief Communication |
Improved low-resolution crystallographic refinement with Phenix and Rosetta
An approach combining the sampling methodology and energy function of Rosetta with the X-ray refinement methodology of Phenix enables improved low-resolution crystallographic refinement.
- Frank DiMaio
- , Nathaniel Echols
- & David Baker
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Brief Communication |
Exploiting tertiary structure through local folds for crystallographic phasing
An algorithm and software tool, Borges, utilizes nonspecific tertiary-structure fragment information available in the Protein Data Bank to phase protein X-ray diffraction data.
- Massimo Sammito
- , Claudia Millán
- & Isabel Usón
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News & Views |
Visualizing networks of mobility in proteins
An algorithm called CONTACT identifies correlated side-chain motions in proteins from X-ray crystallographic data, providing insights into dynamics and function.
- Mark A. Wilson
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Article |
Automated identification of functional dynamic contact networks from X-ray crystallography
An algorithm and software tool to uncover contact networks of interacting conformationally heterogeneous protein residues from X-ray crystallography data is described.
- Henry van den Bedem
- , Gira Bhabha
- & James S Fraser
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Research Highlights |
Magnetic field imaging and more
Two reports demonstrate further advances in the use of nitrogen vacancies for very different imaging applications.
- Daniel Evanko
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Research Highlights |
Metalloenzyme structures in a shot
Researchers study the structure of the metalloenzyme photosystem II by applying femtosecond X-ray pulses to simultaneously record X-ray diffraction and X-ray emission spectroscopy data.
- Allison Doerr
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Article |
Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals
The structure of the membrane anchor domain of the bacterial autotransporter YadA is solved by a solid-state NMR spectroscopy approach using a uniformly 13C- and 15N-labeled microcrystalline sample.
- Shakeel Ahmad Shahid
- , Benjamin Bardiaux
- & Dirk Linke
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News & Views |
Small is beautiful
Using two independent methods, researchers show that in vivo–grown crystals of soluble proteins and of membrane proteins grown in the lipidic sponge phase can be analyzed by serial femtosecond crystallography on an X-ray free electron laser.
- Keith Moffat
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Brief Communication |
Lipidic phase membrane protein serial femtosecond crystallography
Lipidic sponge phase crystallization yields membrane protein microcrystals that can be injected into an X-ray free electron laser beam, yielding diffraction patterns that can be processed to recover the crystal structure.
- Linda C Johansson
- , David Arnlund
- & Richard Neutze
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Brief Communication |
In vivo protein crystallization opens new routes in structural biology
Expression of a protein in Sf9 insect cells at high concentration triggers formation of in vivo crystals that can be analyzed by serial femtosecond X-ray crystallography.
- Rudolf Koopmann
- , Karolina Cupelli
- & Michael Duszenko
AlphaFold predictions are valuable hypotheses and accelerate but do not replace experimental structure determination