9BDJ

MicroED structure of bovine liver catalase with missing cone eliminated by suspended drop

9BDJ の概要

• エントリーDOI: 10.2210/pdb9bdj/pdb
• EMDBエントリー: 44453
• 分子名称: Catalase, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: heme-containing enzyme, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 245444.27

構造登録者

Gillman, C.,Bu, G.,Gonen, T. (登録日: 2024-04-11, 公開日: 2024-09-18, 最終更新日: 2024-10-16)

主引用文献

Gillman, C.,Bu, G.,Danelius, E.,Hattne, J.,Nannenga, B.L.,Gonen, T.
Eliminating the missing cone challenge through innovative approaches.
J Struct Biol X, 9:100102-100102, 2024

PubMed Abstract: Microcrystal electron diffraction (MicroED) has emerged as a powerful technique for unraveling molecular structures from microcrystals too small for X-ray diffraction. However, a significant hurdle arises with plate-like crystals that consistently orient themselves flat on the electron microscopy grid. If the normal of the plate correlates with the axes of the crystal lattice, the crystal orientations accessible for measurement are restricted because the crystal cannot be arbitrarily rotated. This limits the information that can be acquired, resulting in a missing cone of information. We recently introduced a novel crystallization strategy called suspended drop crystallization and proposed that crystals in a suspended drop could effectively address the challenge of preferred crystal orientation. Here we demonstrate the success of the suspended drop approach in eliminating the missing cone in two samples that crystallize as thin plates: bovine liver catalase and the SARS‑CoV‑2 main protease (Mpro). This innovative solution proves indispensable for crystals exhibiting systematic preferred orientations, unlocking new possibilities for structure determination by MicroED.

PubMed: 38962493
DOI: 10.1016/j.yjsbx.2024.100102

実験手法

ELECTRON CRYSTALLOGRAPHY (4 Å)