2g4m

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(New page: 200px<br /><applet load="2g4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g4m, resolution 1.80&Aring;" /> '''Insulin collected at...)
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[[Image:2g4m.jpg|left|200px]]<br /><applet load="2g4m" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2g4m.jpg|left|200px]]<br /><applet load="2g4m" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2g4m, resolution 1.80&Aring;" />
caption="2g4m, resolution 1.80&Aring;" />
'''Insulin collected at 2.0 A wavelength'''<br />
'''Insulin collected at 2.0 A wavelength'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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2G4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G4M OCA].
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2G4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4M OCA].
==Reference==
==Reference==
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Mueller-Dieckmann, C.]]
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[[Category: Weiss, M.S.]]
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[[Category: Weiss, M S.]]
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[[Category: insulin at 2.0 a wavelength]]
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[[Category: insulin at 2 0 a wavelength]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:56:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:03 2008''

Revision as of 15:28, 21 February 2008


2g4m, resolution 1.80Å

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Insulin collected at 2.0 A wavelength

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.

About this Structure

2G4M is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 17:28:03 2008

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