6S2O

Granulovirus occlusion bodies by serial electron diffraction

6S2O の概要

• エントリーDOI: 10.2210/pdb6s2o/pdb
• EMDBエントリー: 10091
• 分子名称: Granulin (2 entities in total)
• 機能のキーワード: granulovirus, occlusion body, serial crystallography, viral protein
• 由来する生物種: Cydia pomonella granulosis virus (isolate Mexico/1963) (CpGV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29378.56

構造登録者

Buecker, R.,Mehrabi, P.,Schulz, E.C.,Hogan-Lamarre, P. (登録日: 2019-06-21, 公開日: 2020-04-29, 最終更新日: 2024-10-23)

主引用文献

Bucker, R.,Hogan-Lamarre, P.,Mehrabi, P.,Schulz, E.C.,Bultema, L.A.,Gevorkov, Y.,Brehm, W.,Yefanov, O.,Oberthur, D.,Kassier, G.H.,Dwayne Miller, R.J.
Serial protein crystallography in an electron microscope.
Nat Commun, 11:996-996, 2020

PubMed Abstract: Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from sub-micron-sized crystals. However, beam time at these facilities is scarce, and involved sample delivery techniques are required. On the other hand, rotation electron diffraction (MicroED) has shown great potential as an alternative means for protein nano-crystallography. Here, we present a method for serial electron diffraction of protein nanocrystals combining the benefits of both approaches. In a scanning transmission electron microscope, crystals randomly dispersed on a sample grid are automatically mapped, and a diffraction pattern at fixed orientation is recorded from each at a high acquisition rate. Dose fractionation ensures minimal radiation damage effects. We demonstrate the method by solving the structure of granulovirus occlusion bodies and lysozyme to resolutions of 1.55 Å and 1.80 Å, respectively. Our method promises to provide rapid structure determination for many classes of materials with minimal sample consumption, using readily available instrumentation.

PubMed: 32081905
DOI: 10.1038/s41467-020-14793-0

実験手法

ELECTRON CRYSTALLOGRAPHY (1.6 Å)