An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage. Serial crystallography offers the prospect of determining low-dose synchrotron or effectively damage free XFEL structures at room temperature and enables time-resolved or dose-resolved approaches. Complementary spectroscopic data can validate redox and or ligand states within metalloprotein crystals. In this opinion, we discuss developments in the application of serial crystallographic approaches to metalloproteins and comment on future directions.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8667872 | PMC |
| http://dx.doi.org/10.1016/j.sbi.2021.07.007 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Convergent-beam attosecond x-ray crystallography.
Struct Dyn
January 2025
Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
Sub-ångström spatial resolution of electron density coupled with sub-femtosecond to few-femtosecond temporal resolution is required to directly observe the dynamics of the electronic structure of a molecule after photoinitiation or some other ultrafast perturbation, such as by soft X-rays. Meeting this challenge, pushing the field of quantum crystallography to attosecond timescales, would bring insights into how the electronic and nuclear degrees of freedom couple, enable the study of quantum coherences involved in molecular dynamics, and ultimately enable these dynamics to be controlled. Here, we propose to reach this realm by employing convergent-beam x-ray crystallography with high-power attosecond pulses from a hard-x-ray free-electron laser.
View Article and Find Full Text PDFThree-dimensional architecture and linearized mapping of vibrissa follicle afferents.
Nat Commun
January 2025
Bernstein Center for Computational Neuroscience Berlin, Humboldt-Universität zu Berlin, Berlin, Germany.
Understanding vibrissal transduction has advanced by serial sectioning and identified afferent recordings, but afferent mapping onto the complex, encapsulated follicle remains unclear. Here, we reveal male rat C2 vibrissa follicle innervation through synchrotron X-ray phase contrast tomograms. Morphological analysis identified 5% superficial, ~32 % unmyelinated and 63% myelinated deep vibrissal nerve axons.
View Article and Find Full Text PDFAdvancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.
Commun Chem
January 2025
ESRF - The European Synchrotron, 71 Avenue des Martyrs, Grenoble, France.
Serial macromolecular crystallography has become a powerful method to reveal room temperature structures of biological macromolecules and perform time-resolved studies. ID29, a flagship beamline of the ESRF 4th generation synchrotron, is the first synchrotron beamline in the world capable of delivering high brilliance microsecond X-ray pulses at high repetition rate for the structure determination of biological macromolecules at room temperature. The cardinal combination of microsecond exposure times, innovative beam characteristics and adaptable sample environment provides high quality complete data, even from an exceptionally small amount of crystalline material, enabling what we collectively term serial microsecond crystallography (SµX).
View Article and Find Full Text PDFScalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography.
Sci Rep
January 2025
Department of Chemical Engineering, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
X-ray crystallography is one of the leading tools to analyze the 3-D structure, and therefore, function of proteins and other biological macromolecules. Traditional methods of mounting individual crystals for X-ray diffraction analysis can be tedious and result in damage to fragile protein crystals. Furthermore, the advent of multi-crystal and serial crystallography methods explicitly require the mounting of larger numbers of crystals.
View Article and Find Full Text PDFReal-time data processing for serial crystallography experiments.
IUCrJ
January 2025
Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany.
We report the use of streaming data interfaces to perform fully online data processing for serial crystallography experiments, without storing intermediate data on disk. The system produces Bragg reflection intensity measurements suitable for scaling and merging, with a latency of less than 1 s per frame. Our system uses the CrystFEL software in combination with the ASAP::O data framework.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!