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Title: A 3.8 Å resolution cryo-EM structure of a small protein bound to an imaging scaffold

Journal Article · · Nature Communications
 [1];  [1];  [2]
  1. Univ. of California, Los Angeles, CA (United States)
  2. Univ. of California, Los Angeles, CA (United States); California NanoSystems Inst., Los Angeles, CA (United States)

Proteins smaller than about 50 kDa are currently too small to be imaged at high resolution by cryo-electron microscopy (cryo-EM), leaving most protein molecules in the cell beyond the reach of this powerful structural technique. Here we use a designed protein scaffold to bind and symmetrically display 12 copies of a small 26 kDa protein, green fluorescent protein (GFP). We show that the bound cargo protein is held rigidly enough to visualize it as a resolution of 3.8 Å by cryo-EM, where specific structural features of the protein are visible. The designed scaffold is modular and can be modified through modest changes in its amino acid sequence to bind and display diverse proteins for imaging, thus providing a general method to break through the lower size limitation in cryo-EM.

Research Organization:
Univ. of California, Los Angeles, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
FC02-02ER63421
OSTI ID:
1609012
Journal Information:
Nature Communications, Vol. 10, Issue 1; ISSN 2041-1723
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 43 works
Citation information provided by
Web of Science

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Cited By (4)

Fragments: where are we now? journal January 2020
Advances in protein structure prediction and design journal August 2019
Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering journal December 2019
Structural analysis of biological targets by host:guest crystal lattice engineering journal October 2019

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