A Rare Lysozyme Crystal Form Solved Using Highly Redundant Multiple Electron Diffraction Datasets from Micron-Sized Crystals
| Autor: | Hugo Lebrette, Taimin Yang, Hongyi Xu, Vivek Srinivas, Sven Hovmöller, Martin Högbom, Xiaodong Zou |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Diffraction Models Molecular Protein Folding Materials science Cryo-electron microscopy Protein Conformation Physics::Optics Datasets as Topic 02 engineering and technology Crystal 03 medical and health sciences Egg White Microscopy Electron Transmission Structural Biology Atomic model Image Processing Computer-Assisted Animals Molecular Biology Crystallography Electron crystallography 021001 nanoscience & nanotechnology Computational physics 030104 developmental biology Electron diffraction Transmission electron microscopy X-ray crystallography Muramidase 0210 nano-technology Crystallization Chickens Software |
| Zdroj: | Structure (London, England : 1993). 26(4) |
| ISSN: | 1878-4186 |
| Popis: | Summary Recent developments of novel electron diffraction techniques have shown to be powerful for determination of atomic resolution structures from micron- and nano-sized crystals, too small to be studied by single-crystal X-ray diffraction. In this work, the structure of a rare lysozyme polymorph is solved and refined using continuous rotation MicroED data and standard X-ray crystallographic software. Data collection was performed on a standard 200 kV transmission electron microscope (TEM) using a highly sensitive detector with a short readout time. The data collection is fast (∼3 min per crystal), allowing multiple datasets to be rapidly collected from a large number of crystals. We show that merging data from 33 crystals significantly improves not only the data completeness, overall I/σ and the data redundancy, but also the quality of the final atomic model. This is extremely useful for electron beam-sensitive crystals of low symmetry or with a preferred orientation on the TEM grid. |
| Databáze: | OpenAIRE |
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