Resolution: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Eric Martz (talk | contribs) No edit summary |
Eric Martz (talk | contribs) No edit summary |
||
| Line 37: | Line 37: | ||
</td></tr></table> | </td></tr></table> | ||
Structure determination by [[X-ray crystallography]] or [[cryo-electron microscopy]] produces an [[electron density map]] (shown | Structure determination by [[X-ray crystallography]] or [[cryo-electron microscopy]] produces an [[electron density map]] (shown in <font color="#508050"><b>green</b></font>). The atomic model, shown as sticks above, is then built, guided by the electron density map. | ||
In X-ray crystallography, resolution is the smallest distance between crystal lattice planes that is resolved in the diffraction pattern. High numeric values of resolution, such as 4 Å, mean poor resolution, while low numeric values, such as 1.5 Å, mean good resolution. | In X-ray crystallography, resolution is the smallest distance between crystal lattice planes that is resolved in the diffraction pattern. High numeric values of resolution, such as 4 Å, mean poor resolution, while low numeric values, such as 1.5 Å, mean good resolution. | ||
