PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7135626

The "EM" program system.

R Hegerl·A Altbauer
View original source ↗Export metadata ↓

Abstract

"EM" is a computer program system concerned with the processing of electron micrographs. It provides facilities for two- and three-dimensional image reconstruction, correlation, filtering, etc. as well as for storage and display of image data. A description of the scientific aims, the system design, and the possibilities to display pictures is given. The handling of the command language is illustrated by some examples.

Explore related subjects

BiopolymersComputersMacromolecular SubstancesMicroscopy, ElectronJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

R Hegerl, A Altbauer. 1982. The "EM" program system.. https://doi.org/10.1016/0304-3991(82)90233-9

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

KEEP EXPLORING

Related citations

PubMed1995

Shaker K+ channel T1 domain self-tetramerizes to a stable structure.

The potassium channel T1 domain plays an important role in the regulated assembly of subunit proteins. We have examined the assembly properties of the Shaker channel T1 domain to determine if the domain can self-assemble, the number of subunits in a multimer, Ns and the mechanism of assembly. High pressure liquid chromatography (HPLC) size exclusion chromotography (SEC) separates T1 domain proteins into two peaks. By co-assembly assays, these peaks are identified to be a high molecular weight assembled form and a low molecular weight monomeric form. To determine the Ns of the assembled protein peak on HPLC SEC, we first cross-linked the T1 domain proteins and then separated them on HPLC. Four evenly spaced bands co-migrate with the assembled protein peak; thus, the T1 domain assembles to form a tetramer. The absence of separate dimeric and trimeric peaks of assembled T1 domain protein suggests that the tetramer is the stable assembled state, most probably a closed ring structure.

Biopolymers↗
PubMed1995

Charge determination of membrane molecules in polymer-supported lipid layers.

A method for two-dimensional micro-electrophoresis and charge determination of fluorescence-labeled membrane molecules in lipid layers is presented. Therefore, the labeled molecules are dissolved in a lipid monolayer which acts as a fluid matrix. The essential part of the sample preparation is an aqueous polymer film composed of agarose onto which the layer is transferred by Langmuir-Blodgett technique. The induced force of an applied electric field leads to a drift of the charged fluorescent molecules. The mobility is determined by an analysis of the steady-state bleach profile which is produced by continuous fluorescence micro-photolysis of a rectangular area of the monolayer. Testing a variety of amphiphilic molecules, measurements yielded values of zero, plus or minus one elementary net charge within a margin of error. The experimental set-up described here can be used for lateral separation, enrichment and isoelectric focusing of membrane components.

Biopolymers↗