| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979125 | Current Opinion in Structural Biology | 2013 | 8 Pages |
•BEVS can provide large multiprotein complexes in high quality and large quantity.•Recent improvements have rendered BEVS easy-to-use, also to non-specialist users.•Recombinant production can overcome limitations caused by sample heterogeneity.•MultiBac BEVS helped to unlock the architecture of complex multiprotein machines.•Structures of Mediator Head, APC/C, MCC, and TFIID core have been determined.
Most essential functions in eukaryotic cells are catalyzed by complex molecular machines built of many subunits. To fully understand their biological function in health and disease, it is imperative to study these machines in their entirety. The provision of many essential multiprotein complexes of higher eukaryotes including humans, can be a considerable challenge, as low abundance and heterogeneity often rule out their extraction from native source material. The baculovirus expression vector system (BEVS), specifically tailored for multiprotein complex production, has proven itself to be uniquely suited for overcoming this impeding bottleneck. Here we highlight recent major achievements in multiprotein complex structure research that were catalyzed by this versatile recombinant complex expression tool.
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