2g4p: Difference between revisions

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New page: left|200px<br /><applet load="2g4p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g4p, resolution 1.84Å" /> '''Anomalous substructu...
 
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[[Image:2g4p.jpg|left|200px]]<br /><applet load="2g4p" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2g4p.jpg|left|200px]]<br /><applet load="2g4p" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2g4p, resolution 1.84&Aring;" />
caption="2g4p, resolution 1.84&Aring;" />
'''Anomalous substructure of lysozyme at pH 4.5'''<br />
'''Anomalous substructure of lysozyme at pH 4.5'''<br />


==Overview==
==Overview==
23 different crystal forms of 19 different biological macromolecules were, examined with respect to their anomalously scattering substructures using, diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more, than 90% of the cases the substructure was found to contain more than just, the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification, protocol are frequently bound to the protein molecule and that these ions, are often overlooked, especially if they are not bound at full occupancy., Thus, in order to fully describe the macromolecule under study, it seems, desirable that any structure determination be complemented with a, long-wavelength data set.
23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.


==About this Structure==
==About this Structure==
2G4P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G4P OCA].  
2G4P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4P OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Weiss, M.S.]]
[[Category: Weiss, M S.]]
[[Category: CL]]
[[Category: CL]]
[[Category: anomalous substructure of lysozyme crystallized at ph 4.5]]
[[Category: anomalous substructure of lysozyme crystallized at ph 4 5]]


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Revision as of 18:28, 21 February 2008

File:2g4p.jpg


2g4p, resolution 1.84Å

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Anomalous substructure of lysozyme at pH 4.5

OverviewOverview

23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.

About this StructureAbout this Structure

2G4P is a Single protein structure of sequence from Gallus gallus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths., Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674

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