6ZET
Crystal structure of proteinase K nanocrystals by electron diffraction with a 20 micrometre C2 condenser aperture
これはPDB形式変換不可エントリーです。
6ZET の概要
| エントリーDOI | 10.2210/pdb6zet/pdb |
| 分子名称 | Proteinase K, CALCIUM ION (2 entities in total) |
| 機能のキーワード | protease, serine protease, hydrolase |
| 由来する生物種 | Parengyodontium album (Tritirachium album) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 28998.87 |
| 構造登録者 | Evans, G.,Zhang, P.,Beale, E.V.,Waterman, D.G. (登録日: 2020-06-16, 公開日: 2020-10-14, 最終更新日: 2024-10-16) |
| 主引用文献 | Beale, E.V.,Waterman, D.G.,Hecksel, C.,van Rooyen, J.,Gilchrist, J.B.,Parkhurst, J.M.,de Haas, F.,Buijsse, B.,Evans, G.,Zhang, P. A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction. Front Mol Biosci, 7:179-179, 2020 Cited by PubMed Abstract: MicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in thickness. Furthermore, traditional microED data processing uses established X-ray crystallography software that is not optimized for handling compound effects that are unique to electron diffraction data. Here, we present an integrated workflow for microED, from sample preparation by cryo-focused ion beam milling, through data collection with a standard Ceta-D detector, to data processing using the DIALS software suite, thus enabling routine atomic structure determination of protein crystals of any size and shape using microED. We demonstrate the effectiveness of the workflow by determining the structure of proteinase K to 2.0 Å resolution and show the advantage of using protein crystal lamellae over nanocrystals. PubMed: 32850967DOI: 10.3389/fmolb.2020.00179 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON CRYSTALLOGRAPHY (2.701 Å) |
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