Electron density maps: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Eric Martz (talk | contribs) |
Eric Martz (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:jmol_edm_tyr_1.0s.png|frame|Snapshot of 1.0 Å electron density map at 1 sigma, displayed in Jmol. [http://www.bioinformatics.org/molvis/edm/ Interactive Version]]] | [[Image:jmol_edm_tyr_1.0s.png|frame|Snapshot of 1.0 Å electron density map at 1 sigma, displayed in Jmol. [http://www.bioinformatics.org/molvis/edm/ Interactive Version]]] | ||
88% of the macromolecular structures available from the | |||
[[Protein Data Bank]] (PDB) | [[Protein Data Bank]] (PDB) | ||
were determined by | were determined by | ||
[[X-ray crystallography]]. The direct results of crystallographic experiments are electron density maps. Examining the correspondence between the electron density map and the published molecular model reveals the levels of uncertainty in the model. | [[X-ray crystallography]] (as of July, 2021). The direct results of crystallographic experiments are electron density maps. Examining the correspondence between the electron density map and the published molecular model reveals the levels of uncertainty in the model. | ||
==Crystallography Produces Electron Density Maps== | ==Crystallography Produces Electron Density Maps== | ||
