Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8YT4

Structure of Aquifex aeolicus Lumazine Synthase by Cryo-Electron Microscopy to 1.42 Angstrom Resolution

8YT4 の概要
エントリーDOI10.2210/pdb8yt4/pdb
EMDBエントリー39478
分子名称6,7-dimethyl-8-ribityllumazine synthase, PHOSPHATE ION (3 entities in total)
機能のキーワードenzyme involved in riboflavin biosynthesis, biosynthetic protein
由来する生物種Aquifex aeolicus
タンパク質・核酸の鎖数1
化学式量合計17864.32
構造登録者
Savva, C.G.,Sobhy, M.A.,De Biasio, A.,Hamdan, S.M. (登録日: 2024-03-24, 公開日: 2024-04-10, 最終更新日: 2024-09-11)
主引用文献Savva, C.G.,Sobhy, M.A.,De Biasio, A.,Hamdan, S.M.
Structure of Aquifex aeolicus lumazine synthase by cryo-electron microscopy to 1.42 angstrom resolution.
Iucrj, 11:723-729, 2024
Cited by
PubMed Abstract: Single-particle cryo-electron microscopy (cryo-EM) has become an essential structural determination technique with recent hardware developments making it possible to reach atomic resolution, at which individual atoms, including hydrogen atoms, can be resolved. In this study, we used the enzyme involved in the penultimate step of riboflavin biosynthesis as a test specimen to benchmark a recently installed microscope and determine if other protein complexes could reach a resolution of 1.5 Å or better, which so far has only been achieved for the iron carrier ferritin. Using state-of-the-art microscope and detector hardware as well as the latest software techniques to overcome microscope and sample limitations, a 1.42 Å map of Aquifex aeolicus lumazine synthase (AaLS) was obtained from a 48 h microscope session. In addition to water molecules and ligands involved in the function of AaLS, we can observe positive density for ∼50% of the hydrogen atoms. A small improvement in the resolution was achieved by Ewald sphere correction which was expected to limit the resolution to ∼1.5 Å for a molecule of this diameter. Our study confirms that other protein complexes can be solved to near-atomic resolution. Future improvements in specimen preparation and protein complex stabilization may allow more flexible macromolecules to reach this level of resolution and should become a priority of study in the field.
PubMed: 38965901
DOI: 10.1107/S2052252524005530
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (1.42 Å)
構造検証レポート
Validation report summary of 8yt4
検証レポート(詳細版)ダウンロードをダウンロード

232418

件を2025-03-05に公開中

PDB statisticsPDBj update infoContact PDBjnumon