High resolution structure of GABAAR beta3 homopentamer
Ontology highlight
ABSTRACT:
SUBMITTER: Sjors Scheres
PROVIDER: EMPIAR-10500 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Single-particle cryo-EM at atomic resolution.
Nakane Takanori T Kotecha Abhay A Sente Andrija A McMullan Greg G Masiulis Simonas S Brown Patricia M G E PMGE Grigoras Ioana T IT Malinauskaite Lina L Malinauskas Tomas T Miehling Jonas J Uchański Tomasz T Yu Lingbo L Karia Dimple D Pechnikova Evgeniya V EV de Jong Erwin E Keizer Jeroen J Bischoff Maarten M McCormack Jamie J Tiemeijer Peter P Hardwick Steven W SW Chirgadze Dimitri Y DY Murshudov Garib G Aricescu A Radu AR Scheres Sjors H W SHW
Nature 20201021 7832
The three-dimensional positions of atoms in protein molecules define their structure and their roles in biological processes. The more precisely atomic coordinates are determined, the more chemical information can be derived and the more mechanistic insights into protein function may be inferred. Electron cryo-microscopy (cryo-EM) single-particle analysis has yielded protein structures with increasing levels of detail in recent years<sup>1,2</sup>. However, it has proved difficult to obtain cryo ...[more]
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