File:Structure-of-Alcohol-Oxidase-from-Pichia-pastoris-by-Cryo-Electron-Microscopy-pone.0159476.s006.ogv
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Summary
DescriptionStructure-of-Alcohol-Oxidase-from-Pichia-pastoris-by-Cryo-Electron-Microscopy-pone.0159476.s006.ogv |
English: The AOX octamer with domain colors shown. Colors are as in Fig 5a: FAD-binding domain (red); FAD covering lid (pink); extended FAD-binding domain (yellow); flavin attachment loop (green) and intermediate region (light green); substrate-binding domain (cyan). Helix H12, which forms crystal contacts, is shown in orange. The longest AOX-specific insert 481–548 is shown in dark blue, other AOX-specific sequences are colored purple. The tetramer interface is exclusively made by AOX-specific elements (dark blue and purple). |
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Date | |||
Source | S5 Movie from Vonck J, Parcej D, Mills D (2016). "Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy". PLOS ONE. DOI:10.1371/journal.pone.0159476. PMID 27458710. PMC: 4961394. | ||
Author | Vonck J, Parcej D, Mills D | ||
Permission (Reusing this file) |
This file is licensed under the Creative Commons Attribution 4.0 International license.
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Items portrayed in this file
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26 July 2016
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current | 02:20, 18 August 2016 | 7.2 s, 822 × 670 (24.19 MB) | Open Access Media Importer Bot | Automatically uploaded media file from Open Access source. Please report problems or suggestions here. |
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Short title | The AOX octamer with domain colors shown. |
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Author | Vonck J, Parcej D, Mills D |
Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | Colors are as in Fig 5a: FAD-binding domain (red); FAD covering lid (pink); extended FAD-binding domain (yellow); flavin attachment loop (green) and intermediate region (light green); substrate-binding domain (cyan). Helix H12, which forms crystal contacts, is shown in orange. The longest AOX-specific insert 481–548 is shown in dark blue, other AOX-specific sequences are colored purple. The tetramer interface is exclusively made by AOX-specific elements (dark blue and purple). |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2016-07-26 |