5OCV
A Rare Lysozyme Crystal Form Solved Using High-Redundancy 3D Electron Diffraction Data from Micron-Sized Needle Shaped Crystals
Summary for 5OCV
Entry DOI | 10.2210/pdb5ocv/pdb |
Descriptor | Lysozyme C, SODIUM ION (3 entities in total) |
Functional Keywords | lysozyme activity, hydrolase |
Biological source | Gallus gallus (Chicken) |
Cellular location | Secreted: P00698 |
Total number of polymer chains | 2 |
Total formula weight | 28685.31 |
Authors | Xu, H.,Lebrette, H.,Yang, T.,Srinivas, V.,Hovmoller, S.,Hogbom, M.,Zou, X. (deposition date: 2017-07-03, release date: 2018-03-28, Last modification date: 2024-11-13) |
Primary citation | Xu, H.,Lebrette, H.,Yang, T.,Srinivas, V.,Hovmoller, S.,Hogbom, M.,Zou, X. A Rare Lysozyme Crystal Form Solved Using Highly Redundant Multiple Electron Diffraction Datasets from Micron-Sized Crystals. Structure, 26:667-675.e3, 2018 Cited by 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 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. PubMed: 29551291DOI: 10.1016/j.str.2018.02.015 PDB entries with the same primary citation |
Experimental method | ELECTRON CRYSTALLOGRAPHY (2.2 Å) |
Structure validation
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