2g55: Difference between revisions
New page: left|200px<br /><applet load="2g55" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g55, resolution 1.82Å" /> '''Anomalous substructu... |
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[[Image:2g55.gif|left|200px]]<br /><applet load="2g55" size=" | [[Image:2g55.gif|left|200px]]<br /><applet load="2g55" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2g55, resolution 1.82Å" /> | caption="2g55, resolution 1.82Å" /> | ||
'''Anomalous substructure of trypsin (P3121)'''<br /> | '''Anomalous substructure of trypsin (P3121)'''<br /> | ||
==Overview== | ==Overview== | ||
23 different crystal forms of 19 different biological macromolecules were | 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== | ||
2G55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http:// | 2G55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G55 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Mueller-Dieckmann, C.]] | [[Category: Mueller-Dieckmann, C.]] | ||
[[Category: Weiss, M | [[Category: Weiss, M S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: anomalous substructure of trypsin (p3121)]] | [[Category: anomalous substructure of trypsin (p3121)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:13 2008'' |
Revision as of 18:28, 21 February 2008
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Anomalous substructure of trypsin (P3121)
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
2G55 is a Single protein structure of sequence from Bos taurus with and as ligands. Active as Trypsin, with EC number 3.4.21.4 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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