Resolution: Difference between revisions
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At 0.5 Å in the movie, every atom<ref name="stills" /> of the tryptophan sidechain in the top center of the frame is clearly represented by a sphere of electron density. At 2.5 Å (a bit worse than the median in the [[PDB]]), the overall shape and position of the Trp sidechain is still clear, as is the alpha helical conformation of the main chain. However, at 5.0 Å, only an ill-fitting bump is present to signal the bulky Trp sidechain, and the alpha helix becomes a cylinder of electron density, from which the handedness of the helix may not be | At 0.5 Å in the movie, every atom<ref name="stills" /> of the tryptophan sidechain in the top center of the frame is clearly represented by a sphere of electron density. At 2.5 Å (a bit worse than the median in the [[PDB]]), the overall shape and position of the Trp sidechain is still clear, as is the alpha helical conformation of the main chain. However, at 5.0 Å, only an ill-fitting bump is present to signal the bulky Trp sidechain, and the alpha helix becomes a cylinder of electron density, from which the handedness of the helix may not be discernible. | ||
Once refinement of the electron density map is completed, the amount of electron density at the position of each atom determines that atom's [Temperature|B factor or temperature value]. | |||
==See Also== | ==See Also== | ||
