Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase

Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase

The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododec...

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Bibliographic Details
Main Authors: Appolaire, Alexandre, Girard, Eric, Colombo, Matteo, Durá, M. Asunción, Moulin, Martine, Härtlein, Michael, Franzetti, Bruno, Gabel, Frank
Format: Online
Language:English
Published: International Union of Crystallography 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220976/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220976/

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