Item

ITEM ACTIONS

This item is discarded!Release HistoryDetailsSummary

Discarded

Journal Article

Revisiting the structure of haemoglobin and myoglobin with cryo-electron microscopy.

MPS-Authors

/persons/resource/persons127963

Khoshouei, Maryam
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons123013

Danev, Radostin
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78517

Plitzko, Jürgen M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77721

Baumeister, Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Khoshouei, M., Danev, R., Plitzko, J. M., & Baumeister, W. (2017). Revisiting the structure of haemoglobin and myoglobin with cryo-electron microscopy. Journal of Molecular Biology, 429(17), 2611-2618. doi:10.1016/j.jmb.2017.07.004.

Abstract

Sixty years ago the first protein structure was determined by John Kendrew and his colleagues, that of myoglobin; haemoglobin followed shortly thereafter. For quite some time it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo- electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins which span a size range from several megadaltons to proteins as small as myoglobin and haemoglobin. Copyright 2017. Published by Elsevier Ltd.