Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Cryo-electron microscopy reveals an ATP-fueled and Integrin-I mediated conformational transition of the AAA+ activation complex in R. capsulatus Mg-chelatase
Dept. of Molecular Biophysics, Lund University.
KTH, School of Technology and Health (STH), Structural Biotechnology.
Division of Metabolic Diseases, Karolinska Institutet.
Dept. of Biochemistry, Lund University.
Show others and affiliations
(English)Manuscript (Other academic)
Keyword [en]
cryo-EM, single-particle, reconstruction, alignment, AAA, BchI, BchD, BchH, Mg-chelatase
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-8112OAI: oai:DiVA.org:kth-8112DiVA: diva2:13344
Note
QC 20100719Available from: 2008-03-18 Created: 2008-03-18 Last updated: 2010-10-04Bibliographically approved
In thesis
1. Protein structure dynamics and interplay: by single-particle electron microscopy
Open this publication in new window or tab >>Protein structure dynamics and interplay: by single-particle electron microscopy
2008 (English)Doctoral thesis, comprehensive summary (Other scientific)
Abstract [en]

Single-particle cryo-electron microscopy (cryo-EM) is a method capable of obtaining information about the structural organization and dynamics of large macromolecular assemblies. In the late nineties, the method was suggested to have the potential of generating “atomic resolution” reconstructions of particles above a certain mass. However, visualization of secondary structure elements in cryo-EM reconstructions has so far been achieved mainly for highly symmetrical macromolecular assemblies or by using previously existing X-ray structures to solve the initial alignment problem. A factor that severely limits the resolution for low-symmetry (point group symmetry Cn) particles is the problem of ab initio three-dimensional alignment of cryo-EM projection images of proteins in vitreous ice.

A more general problem in the field of molecular biology is the study of heterogeneous structural properties of particles in preparations of purified macromolecular complexes. If not resolved, structural heterogeneity limits the achievable resolution of a cryo-EM reconstruction and makes correct biological interpretation difficult. If resolved, the heterogeneity instead offers a tremendous biological insight into the dynamic behaviour of a structure, and statistical information about partitioning over subpopulations with distinct structural features within the ensemble of particles may be gained.

This thesis adds to the existing body of methods in the field of single-particle cryo-EM by addressing the problem of ab initio rotational alignment and the problem of resolving structural heterogeneity without using a priori information about the structural variability within large populations of cryo-EM projections of unstained proteins. The thesis aims at making the single-particle cryo-EM method a generally applicable tool for generating subnanometer resolution reconstructions and perform heterogeneity analysis of biological macromolecules.

Place, publisher, year, edition, pages
Stockholm: KTH, 2008. 83 p.
Series
Trita-STH : report, ISSN 1653-3836 ; 2008:1
Keyword
biophysics, biochemistry, molecular
National Category
Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-4669 (URN)978-91-7178-892-4 (ISBN)
Public defence
2008-04-04, Hörsallen plan 4, Novum, Flemingsberg, Huddinge, 13:00
Opponent
Supervisors
Note
QC 20100719Available from: 2008-03-18 Created: 2008-03-18 Last updated: 2010-10-01Bibliographically approved

Open Access in DiVA

No full text

Authority records BETA

Hebert, Hans

Search in DiVA

By author/editor
Elmlund, HansHebert, HansLindahl, Martin
By organisation
Structural Biotechnology
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 88 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf