Abstract
Knowledge of protein crystal perfection in theory and practice is reviewed. X-ray methods of assessing perfection such as mosaicity, topography and reciprocal-space mapping are described. X-ray diffraction physics applications of protein crystals such as in Laue geometry, the large-angle oscillation technique and forming polychromatic profiles across diffraction spots are covered. Cryo- and room-temperature cases are discussed including in X-ray and neutron protein crystallography. Experience of freezing very large crystals, which are commonly used today in neutron protein crystallography, is highlighted. © 2005 International Union of Crystallography - all rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 793-798 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 61 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jun 2005 |