Abstract
Cryogenic electron microscopy (cryo-EM) and single-particle analysis now enables the determination of high-resolution structures of macromolecular assemblies that have resisted X-ray crystallography and other approaches. Successful high-resolution structure determination by cryo-EM always depends on the quality of the protein sample. While structural heterogeneity remains a key challenge for cryo-EM, it also represents a rare opportunity to study the intrinsic conformational flexibility of macromolecular assemblies. Here, we review the key technological advancements that have made this ‘resolution revolution’ possible and give a concise overview of the technical challenges that needed to be overcome to allow high-resolution structure determination.
| Original language | English |
|---|---|
| Number of pages | 6 |
| Journal | Current Opinion in Structural Biology |
| Volume | 46 |
| DOIs | |
| Publication status | Published - 1 Oct 2017 |
Cite this
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High-resolution cryo-EM : the nuts and bolts. / Elmlund, Dominika; Le, Sarah N; Elmlund, Hans.
In: Current Opinion in Structural Biology, Vol. 46, 01.10.2017.Research output: Contribution to journal › Review Article › Research › peer-review
TY - JOUR
T1 - High-resolution cryo-EM
T2 - the nuts and bolts
AU - Elmlund, Dominika
AU - Le, Sarah N
AU - Elmlund, Hans
PY - 2017/10/1
Y1 - 2017/10/1
N2 - Cryogenic electron microscopy (cryo-EM) and single-particle analysis now enables the determination of high-resolution structures of macromolecular assemblies that have resisted X-ray crystallography and other approaches. Successful high-resolution structure determination by cryo-EM always depends on the quality of the protein sample. While structural heterogeneity remains a key challenge for cryo-EM, it also represents a rare opportunity to study the intrinsic conformational flexibility of macromolecular assemblies. Here, we review the key technological advancements that have made this ‘resolution revolution’ possible and give a concise overview of the technical challenges that needed to be overcome to allow high-resolution structure determination.
AB - Cryogenic electron microscopy (cryo-EM) and single-particle analysis now enables the determination of high-resolution structures of macromolecular assemblies that have resisted X-ray crystallography and other approaches. Successful high-resolution structure determination by cryo-EM always depends on the quality of the protein sample. While structural heterogeneity remains a key challenge for cryo-EM, it also represents a rare opportunity to study the intrinsic conformational flexibility of macromolecular assemblies. Here, we review the key technological advancements that have made this ‘resolution revolution’ possible and give a concise overview of the technical challenges that needed to be overcome to allow high-resolution structure determination.
UR - http://www.scopus.com/inward/record.url?scp=85015845117&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2017.03.003
DO - 10.1016/j.sbi.2017.03.003
M3 - Review Article
AN - SCOPUS:85015845117
VL - 46
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
SN - 0959-440X
ER -