Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2001 Aug 6;154(3):611–618. doi: 10.1083/jcb.200105079

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2001, The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 2. — Transverse sections (z-sections) of 3-D reconstructions. (a) F-actin control. Because adjacent actin monomers are staggered by ∼1/2 × 55 Å, sectioning the reconstruction through the widest part of one actin (monomer on the right) results in sectioning through a narrower part of the adjacent one (on the left); outer and inner domains are marked A_o and A_i on each. (b) F-actin–MLCK-147; note the extra density (arrow) due to MLCK on the extreme periphery of the map bridging inner and outer domains of the two actin monomers sectioned. (c) Maps in a and b were compared, and the difference between the two (filled black region) was superimposed on a copy of the F-actin map. The difference densities, attributable to the bound MLCK, were statistically significant at >99.95% confidence levels. This analysis also showed that the protein-free pore between the MLCK density and F-actin (* in b; cross-hatching in c) was negatively significant, as if decorated filaments drew in extra stain in this region. Sections shown are at the same axial position and have the same relative orientation. The average phase residual (Ψ ± SD), a measurement of the geometrical agreement among filaments generating reconstructions, was 54.0 ± 5.9° for the F-actin–MLCK-147 data. The average up–down phase residual (ΔΨ ± SD), a measure of filament polarity, was 23.7 ± 8.5°. The two values were comparable to those previously obtained.