2g4k: Difference between revisions

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==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==

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[[Category: Single protein]]

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

[[Category: Weiss, M.S.]]

[[Category: Weiss, M S.]]

[[Category: CL]]

[[Category: MG]]

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[[Category: hydrolase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:05 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Mueller-Dieckmann, C.]]
-[[Category: Weiss, M.S.]]
+[[Category: Weiss, M S.]]
 [[Category: CL]]
 [[Category: MG]]
@@ Line 20: / Line 20: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:27:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:05 2008''