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| Title | A Rare Lysozyme Crystal Form Solved Using Highly Redundant Multiple Electron Diffraction Datasets from Micron-Sized Crystals. |
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| Journal, issue, pages | Structure, Vol. 26, Issue 4, Page 667-675.e3, Year 2018 |
| Publish date | Apr 3, 2018 |
 Authors | Hongyi Xu / Hugo Lebrette / Taimin Yang / Vivek Srinivas / Sven Hovmöller / Martin Högbom / Xiaodong Zou /  |
| PubMed Abstract | 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 ...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. |
 External links | Structure / PubMed:29551291 |
| Methods | EM (electron crystallography) |
| Resolution | 2.2 Å |
| Structure data |  PDB-5ocv: |
| Chemicals |  ChemComp-NA:  ChemComp-HOH: |
| Source |
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 Keywords | HYDROLASE / Lysozyme activity |
gallus gallus (chicken)