Resolution: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Eric Martz (talk | contribs) No edit summary |
Eric Martz (talk | contribs) |
||
| Line 65: | Line 65: | ||
If some portions of the macromolecule are less ordered in the crystal than others, these will have a poorer resolution. The "resolution of the crystal" represents the most ordered portions. | If some portions of the macromolecule are less ordered in the crystal than others, these will have a poorer resolution. The "resolution of the crystal" represents the most ordered portions. | ||
==Resolution of a reflection vs. resolution of a diffraction data set== | |||
Each diffraction spot (also called "reflection" or "measurement") in a diffraction pattern has a nominal resolution. The higher the diffraction angle (i.e. the further from the center of the diffraction image where the incoming X-ray beam would hit), the higher the resolution. In a diffraction experiment, the goal is to collect as many reflections as possible. However, reflections of high resolution are more difficult to measure because the intensity of reflections drops off at higher diffraction angles (and with that, higher resolution). In a diffraction image, you will see high intensity spots near the center, and more and more faded spots as you move away from the center. The overall resolution of a diffraction data set refers to the resolution range of reflections measured. For example, "data were collected from 20.0 Å to 2.3 Å with an overall completeness of 96.5%" means that most reflections in this range were collected, and the data set would be described in brief as "2.3 Å resolution" data set, referring to the high resolution limit of the data collection. | |||
==See Also== | ==See Also== | ||
