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TitleBelow 3 Å structure of apoferritin using a multipurpose TEM with a side entry cryoholder.
Journal, issue, pagesSci Rep, Vol. 11, Issue 1, Page 8395, Year 2021
Publish dateApr 16, 2021
AuthorsYoko Kayama / Raymond N Burton-Smith / Chihong Song / Naoya Terahara / Takayuki Kato / Kazuyoshi Murata /
PubMed AbstractRecently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA ...Recently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA are based on data acquired on state-of-the-art cryo-electron microscopes customized for SPA. These are currently only available in limited locations around the world, where securing machine time is highly competitive. One potential solution for this time-competitive situation is to reuse existing multi-purpose equipment, although this comes with performance limitations. Here, a multi-purpose TEM with a side entry cryo-holder was used to evaluate the potential of high-resolution SPA, resulting in a 3 Å resolution map of apoferritin with local resolution extending to 2.6 Å. This map clearly showed two positions of an aromatic side chain. Further, examination of optimal imaging conditions depending on two different multi-purpose electron microscope and camera combinations was carried out, demonstrating that higher magnifications are not always necessary or desirable. Since automation is effectively a requirement for large-scale data collection, and augmenting the multi-purpose equipment is possible, we expanded testing by acquiring data with SerialEM using a β-galactosidase test sample. This study demonstrates the possibilities of more widely available and established electron microscopes, and their applications for cryo-EM SPA.
External linksSci Rep / PubMed:33863933 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 5.1 Å
Structure data

EMDB-30095:
3.6A beta-galactosidase using JEM-2100F + K2 Summit, SerialEM acquisition, RELION 3.0 processing.
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-30096:
3A Apoferritin, JEM-2100F + K2 Summit, 50K, RELION 3.1
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-30097:
3.3A apoferritin from JEM-2100F + K2 Summit at 50K with symmetry expansion.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-30098:
3.3A apoferritin from JEM-2100F + K2 Summit at 50K with octahedral symmetry.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-30099:
3.9A apoferritin from JEM-2100F + K2 Summit at 60K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-30100:
3.4A apoferritin from JEM-2100F + K2 Summit at 40K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-30101:
4A apoferritin from JEM-2100F + K2 Summit at 30K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-30103:
4.5A apoferritin from JEM-2200FS + DE-20 at 40K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-30105:
3.8A apoferritin from JEM-2200FS + DE-20 at 60K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-30106:
3.9A apoferritin from JEM-2200FS + DE-20 at 80K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-30107:
5.1A apoferritin from JEM-2200FS + DE-20 at 100K, RELION 3.0 processing, manual acquisition.
Method: EM (single particle) / Resolution: 5.1 Å

Source
  • Escherichia coli (E. coli)
  • Mus musculus (house mouse)

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