Results 81 to 90 of about 470,172 (244)
Cryocrystallography is a widely used method for determining the crystal structure of macromolecules. This technique uses a cryoenvironment, which significantly reduces the radiation damage to the crystals and has the advantage of requiring only one ...
Ki Hyun Nam
doaj +1 more source
Direct Evidence of Topological Dirac Fermions in a Low Carrier Density Correlated 5d Oxide
The 5d oxide BiRe2O6 is discovered as a low‐carrier‐density topological semimetal hosting symmetry‐protected Dirac fermions stabilized by nonsymmorphic symmetries. Angle‐resolved photoemission spectroscopy, quantum oscillations, and magnetotransport measurements reveal gapless Dirac cones, quasi‐2D Fermi surfaces, high carrier mobility, and a field ...
Premakumar Yanda +11 more
wiley +1 more source
Multiple Twinning in Nacre and Aragonite
Electron backscatter diffraction map of a cluster of geologic aragonite, exhibiting single, double, and triple twins. The whole cluster is approximately 2 cm wide. Colors indicate crystal orientations, so that pixels where the a‐, b‐, and c‐axis is perpendicular to the image plane are green, red, and blue, respectively.
Connor A. Schmidt +7 more
wiley +1 more source
Standard Sample Preparation for Serial Femtosecond Crystallography
The development of serial crystallography (SX), including serial synchrotron crystallography (SSX) at synchrotron sources and serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs), has facilitated the collection of high ...
Christina Schmidt +3 more
doaj +1 more source
Apatite occurs in many forms in nature, e.g. in teeth and geological minerals. Internally, biological apatite contains nanocrystals that are also found in synthetically prepared calcium phosphate nanoparticles which are used in biomedicine, e.g. for gene and drug delivery and for bone regeneration. Abstract Calcium phosphate is the inorganic component (
Kathrin Kostka +3 more
wiley +1 more source
Time-resolved structural studies with serial crystallography: A new light on retinal proteins
Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy.
Valérie Panneels +17 more
doaj +1 more source
Identification of rogue datasets in serial crystallography [PDF]
Advances in beamline optics, detectors and X-ray sources allow new techniques of crystallographic data collection. In serial crystallography, a large number of partial datasets from crystals of small volume are measured. Merging of datasets from different crystals in order to enhance data completeness and accuracy is only valid if the crystals are ...
Assmann, Greta M. +2 more
openaire +3 more sources
In situ TEM uncovers the atomic‐scale mechanisms underlying hydrogen‐driven γ‐Fe2O3→Fe3O4→FeO reduction. In γ‐Fe2O3, oxygen vacancies cluster around intrinsic Fe vacancies, leading to nanopore formation, whereas in Fe3O4, vacancy aggregation is suppressed, preserving a dense structure.
Yupeng Wu +14 more
wiley +1 more source
Sample Delivery Media for Serial Crystallography [PDF]
X-ray crystallographic methods can be used to visualize macromolecules at high resolution. This provides an understanding of molecular mechanisms and an insight into drug development and rational engineering of enzymes used in the industry. Although conventional synchrotron-based X-ray crystallography remains a powerful tool for understanding molecular
openaire +2 more sources
The Anisotropic Adsorption of De Novo Allosteric Two‐Component Protein Fibers on Mica Surfaces
In this study, the interfacial behavior of de novo designed proteins that self‐assemble into tubular architectures with distinct morphologies — small (S), large (L), and helical (H) fibers — at the muscovite mica‐water interface is explored using in situ AFM. Abstract Protein adsorption at solid–liquid interfaces underlies many biomedical and materials
Chenyang Shi +7 more
wiley +1 more source

