1ejg
From Proteopedia
(New page: 200px<br /><applet load="1ejg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejg, resolution 0.54Å" /> '''CRAMBIN AT ULTRA-HIG...) |
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| - | [[Image:1ejg.gif|left|200px]]<br /><applet load="1ejg" size=" | + | [[Image:1ejg.gif|left|200px]]<br /><applet load="1ejg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ejg, resolution 0.54Å" /> | caption="1ejg, resolution 0.54Å" /> | ||
'''CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.'''<br /> | '''CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The charge density distribution of a protein has been refined | + | The charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 A) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1EJG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http:// | + | 1EJG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lecomte, C.]] | [[Category: Lecomte, C.]] | ||
[[Category: Pichon-Lesme, V.]] | [[Category: Pichon-Lesme, V.]] | ||
| - | [[Category: Teeter, M | + | [[Category: Teeter, M M.]] |
[[Category: multi-substate]] | [[Category: multi-substate]] | ||
[[Category: multipole refinement]] | [[Category: multipole refinement]] | ||
[[Category: valence electron density]] | [[Category: valence electron density]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:24 2008'' |
Revision as of 10:28, 21 February 2008
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CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.
Overview
The charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 A) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules.
About this Structure
1EJG is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.
Reference
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin., Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C, Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3171-6. PMID:10737790
Page seeded by OCA on Thu Feb 21 12:28:24 2008
