Examples of electron density: Difference between revisions
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== Figures from Bernhard Rupp's book "Biomolecular Crystallography" (with permission by the author) == | == Figures from Bernhard Rupp's book "Biomolecular Crystallography" (with permission by the author) == | ||
There is more material (all figures, citations, tutorials) at the [http://www.ruppweb.org/garland/ book's overview page]. | |||
You can see the full-size, high-resolution figure by clicking on it. | You can see the full-size, high-resolution figure by clicking on it. | ||
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=== Cis-peptide bond and its electron density === | === Cis-peptide bond and its electron density === | ||
[[File:BMC 2-9.jpg|1024px]] | [[File:BMC 2-9.jpg|1024px]] | ||
---- | |||
=== Covalently modified residues === | === Covalently modified residues === | ||
[[File:BMC 2-27.JPG|1024px]] | [[File:BMC 2-27.JPG|1024px]] | ||
---- | |||
=== Covalent binding of ligands === | === Covalent binding of ligands === | ||
[[File:BMC 2-30.jpg|1024px]] | [[File:BMC 2-30.jpg|1024px]] | ||
---- | |||
=== Additives mediating intermolecular contacts === | === Additives mediating intermolecular contacts === | ||
| Line 20: | Line 28: | ||
=== Heavy-atom derivatization of a protein === | === Heavy-atom derivatization of a protein === | ||
[[File:BMC 3-42.jpg|1024px]] | [[File:BMC 3-42.jpg|1024px]] | ||
---- | |||
=== The trimeric bacterial outer membrane protein OprP === | === The trimeric bacterial outer membrane protein OprP === | ||
| Line 28: | Line 38: | ||
[[File:BMC 4-19.jpg|1024px]] | [[File:BMC 4-19.jpg|1024px]] | ||
---- | |||
=== Glycosylated residues stabilizing homodimer === | === Glycosylated residues stabilizing homodimer === | ||
[[File:BMC 4-20.jpg|1024px]] | [[File:BMC 4-20.jpg|1024px]] | ||
---- | |||
=== Uranium-atom solution and Fourier truncation ripples === | === Uranium-atom solution and Fourier truncation ripples === | ||
[[File:BMC 10-10.jpg|1024px]] | [[File:BMC 10-10.jpg|1024px]] | ||
---- | |||
=== Solvent molecules (water, MPD, Mg2+) === | === Solvent molecules (water, MPD, Mg2+) === | ||
[[File:BMC 12-30.JPG|1024px]] | [[File:BMC 12-30.JPG|1024px]] | ||
(Pete Dunten had noticed that PDB code 2nls should be 1nls; this is now in the [http://www.ruppweb.org/garland/errata.htm book's errata]; the above legend has the correction.) | |||
---- | |||
=== Split side-chain conformations === | === Split side-chain conformations === | ||
[[File:BMC 12-33.JPG|1024px]] | [[File:BMC 12-33.JPG|1024px]] | ||
---- | |||
=== Se-Met residues and chloride ion === | === Se-Met residues and chloride ion === | ||
Latest revision as of 15:09, 19 July 2010
Figures from Bernhard Rupp's book "Biomolecular Crystallography" (with permission by the author)[edit | edit source]
There is more material (all figures, citations, tutorials) at the book's overview page.
You can see the full-size, high-resolution figure by clicking on it.
Cis-peptide bond and its electron density[edit | edit source]
Covalently modified residues[edit | edit source]
Covalent binding of ligands[edit | edit source]
Additives mediating intermolecular contacts[edit | edit source]
Heavy-atom derivatization of a protein[edit | edit source]
The trimeric bacterial outer membrane protein OprP[edit | edit source]
Chemically modified lysine residue (Dimethyllysine)[edit | edit source]
Glycosylated residues stabilizing homodimer[edit | edit source]
Uranium-atom solution and Fourier truncation ripples[edit | edit source]
Solvent molecules (water, MPD, Mg2+)[edit | edit source]
(Pete Dunten had noticed that PDB code 2nls should be 1nls; this is now in the book's errata; the above legend has the correction.)
Split side-chain conformations[edit | edit source]
Se-Met residues and chloride ion[edit | edit source]
