Search PubMed⌕ Search
Home/Archive/PubMed

PubMed · 3225656

High-resolution electron microscopy image simulation on a Cray 1S/2300 computer.

R Spycher·P Stadelmann·P Buffat·M Flueli
View original source ↗Export metadata ↓

Abstract

High-resolution electron microscopy (HREM) image simulation by the multislice method has been implemented on a Cray 1S/2300 computer, allowing accurate full nonlinear image intensity calculations with possible sampling up to 2n x 2m samples of the transmission function (n + m = 20). As examples of applications, images have been obtained from an interface in PbTiO3 and of a small gold aggregate. HREM image simulation of perfect or faulted crystals can now be applied with reasonable computing times to problems involving a large number of atoms and thick or large supercells.

Explore related subjects

CrystallizationGoldImage Processing, Computer-AssistedMathematicsMicroscopy, ElectronMolecular StructureJournal ArticleResearch Support, Non-U.S. Gov't

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

R Spycher, P Stadelmann, P Buffat, M Flueli. 1988. High-resolution electron microscopy image simulation on a Cray 1S/2300 computer.. https://doi.org/10.1002/jemt.1060100403

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Core-controlled polymorphism in virus-like particles.

This study concerns the self-assembly of virus-like particles (VLPs) composed of an icosahedral virus protein coat encapsulating a functionalized spherical nanoparticle core. The recent development of efficient methods for VLP self-assembly has opened the way to structural studies. Using electron microscopy with image reconstruction, the structures of several VLPs obtained from brome mosaic virus capsid proteins and gold nanoparticles were elucidated. Varying the gold core diameter provides control over the capsid structure. The number of subunits required for a complete capsid increases with the core diameter. The packaging efficiency is a function of the number of capsid protein subunits per gold nanoparticle. VLPs of varying diameters were found to resemble to three classes of viral particles found in cells (T=1, 2, and 3). As a consequence of their regularity, VLPs form three-dimensional crystals under the same conditions as the wild-type virus. The crystals represent a form of metallodielectric material that exhibits optical properties influenced by multipolar plasmonic coupling.

Crystallization↗