Protein electron crystallography by 400kV cryo-microscopy
| Autor: | Jaap Brink, Michael F. Schmid, Toshinori Soejima, Wah Chiu |
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| Rok vydání: | 1992 |
| Předmět: | |
| Zdroj: | Proceedings, annual meeting, Electron Microscopy Society of America. 50:1054-1055 |
| ISSN: | 2690-1315 0424-8201 |
| DOI: | 10.1017/s0424820100129905 |
| Popis: | Protein electron crystallography can provide a reconstruction detailed enough for the polypeptide chain of a membrane protein to be traced (1). However, there remain a number of technical problems associated with this technique that must be overcome before it can become a routine tool for high resolution three-dimensional structural analysis of protein crystals. A 400 kV electron microscope has been demonstrated to be advantageous for enhancement of resolution and contrast in images of protein crystals (1,2) because of a reduction in chromatic aberration effects. This paper addresses the question of experimental strategy in data collection for thin protein crystals with a 400 kV cryo-microscope. We will use crotoxin complex and T4 DNA helix destabilizing protein as examples of thin crystals to illustrate our approach.Crotoxin complex forms highly ordered crystals with different thicknesses among different crystals. In order to simplify sorting out data from the various crystals for 3-dimensional merging, it is desirable to collect as much data as possible from a single crystal. |
| Databáze: | OpenAIRE |
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