2g4x: Difference between revisions

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[[Image:2g4x.~~jpg~~|left|200px]]

[[Image:2g4x.png|left|200px]]

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~~'''~~Anomalous substructure od ribonuclease A (P3221)~~'''~~

===Anomalous substructure od ribonuclease A (P3221)===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17327674}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17327674 is the PubMed ID number.

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==About this Structure==

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[[Category: Mueller-Dieckmann, C.]]

[[Category: Weiss, M S.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:41:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:40:40 2008''

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-[[Image:2g4x.jpg|left|200px]]
+{{Seed}}
+[[Image:2g4x.png|left|200px]]
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 {{STRUCTURE_2g4x|  PDB=2g4x  |  SCENE=  }}
-'''Anomalous substructure od ribonuclease A (P3221)'''
+===Anomalous substructure od ribonuclease A (P3221)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17327674}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17327674 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17327674}}
 ==About this Structure==
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 [[Category: Mueller-Dieckmann, C.]]
 [[Category: Weiss, M S.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:41:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:40:40 2008''