Document Type

Article

Publication Date

2017

DOI

10.1155/2017/1793213

Publication Title

Biomed Research International

Volume

2017

Issue

Article ID 1793213

Pages

1-9

Abstract

Cryo-electron microscopy (cryo-EM) has produced density maps of various resolutions. Although ά-helices can be detected from density maps at 5-8 angstrom resolutions, β-strands are challenging to detect at such density maps due to close-spacing of β-strands. The variety of shapes of β-sheets adds the complexity of β-strands detection from density maps. We propose a new approach to model traces of β-strands for β-barrel density regions that are extracted from cryo-EM density maps. In the test containing eight β-barrels extracted from experimental cryo-EM density maps at 5.5 angstrom-8.25 angstrom resolution, StrandRoller detected about 74.26% of the amino acids in the β-strands with an overall 2.05 angstrom 2-way distance between the detected β-traces and the observed ones, if the best of the fifteen detection cases is considered.

Original Publication Citation

Si, D., & He, J. (2017). Modeling beta-traces for beta-barrels from cryo-EM density maps. BioMed Research International, 2017 (#1793213): 1-9. doi: 10.1155/2017/1793213

ORCID

0000-0002-7249-4746 (He)

Download

Share

COinS