Abstract
In protein electron crystallography, both low dose electron diffraction patterns and images are needed to provide accurate amplitudes and phases respectively for a 3-dimensional reconstruction. A limitation of the slow scan CCD camera for recording electron images of protein crystals arises from the relatively large pixel size. The modulation transfer function of the camera with a P43 scintillator has been determined for 400 keV electrons and show an amplitude fall-off. In order to evaluate the structural resolution that the camera can deliver in imaging protein crystals, the ice-embedded catalase crystal was used as a test specimen.
| Original language | English (US) |
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| Pages | 98-99 |
| Number of pages | 2 |
| State | Published - 1994 |
| Externally published | Yes |
| Event | Proceedings of the 52nd Annual Meeting of the Microscopy Society of America - New Orleans, LA, USA Duration: Jul 31 1994 → Aug 5 1994 |
Other
| Other | Proceedings of the 52nd Annual Meeting of the Microscopy Society of America |
|---|---|
| City | New Orleans, LA, USA |
| Period | 7/31/94 → 8/5/94 |
ASJC Scopus subject areas
- General Engineering