1hj8: Difference between revisions
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==Overview== | ==Overview== | ||
Radiation damage is an inherent problem in protein X-ray crystallography, and the process has recently been shown to be highly specific, exhibiting, features such as cleavage of disulfide bonds, decarboxylation of acidic, residues, increase in atomic B factors and increase in unit-cell volume., Reported here are two trypsin structures at atomic resolution (1.00 and, 0.95 A), the data for which were collected at a third-generation, synchrotron (ESRF) at two different beamlines. Both trypsin structures, exhibit broken disulfide bonds; in particular, the bond from Cys191 to, Cys220 is very sensitive to synchrotron radiation. The data set collected, at the most intense beamline (ID14-EH4) shows increased structural, radiation damage in terms of lower occupancies for cysteine residues, more, .. | Radiation damage is an inherent problem in protein X-ray crystallography, and the process has recently been shown to be highly specific, exhibiting, features such as cleavage of disulfide bonds, decarboxylation of acidic, residues, increase in atomic B factors and increase in unit-cell volume., Reported here are two trypsin structures at atomic resolution (1.00 and, 0.95 A), the data for which were collected at a third-generation, synchrotron (ESRF) at two different beamlines. Both trypsin structures, exhibit broken disulfide bonds; in particular, the bond from Cys191 to, Cys220 is very sensitive to synchrotron radiation. The data set collected, at the most intense beamline (ID14-EH4) shows increased structural, radiation damage in terms of lower occupancies for cysteine residues, more, breakage in the six disulfide bonds and more alternate conformations. It, appears that high intensity and not only the total X-ray dose is most, harmful to protein crystals. | ||
==About this Structure== | ==About this Structure== | ||
1HJ8 is a | 1HJ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmo_salar Salmo salar] with SO4, CA and BAM 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] Structure known Active Site: CA1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HJ8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: trypsin]] | [[Category: trypsin]] | ||
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Revision as of 14:59, 5 November 2007
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1.00 AA TRYPSIN FROM ATLANTIC SALMON
OverviewOverview
Radiation damage is an inherent problem in protein X-ray crystallography, and the process has recently been shown to be highly specific, exhibiting, features such as cleavage of disulfide bonds, decarboxylation of acidic, residues, increase in atomic B factors and increase in unit-cell volume., Reported here are two trypsin structures at atomic resolution (1.00 and, 0.95 A), the data for which were collected at a third-generation, synchrotron (ESRF) at two different beamlines. Both trypsin structures, exhibit broken disulfide bonds; in particular, the bond from Cys191 to, Cys220 is very sensitive to synchrotron radiation. The data set collected, at the most intense beamline (ID14-EH4) shows increased structural, radiation damage in terms of lower occupancies for cysteine residues, more, breakage in the six disulfide bonds and more alternate conformations. It, appears that high intensity and not only the total X-ray dose is most, harmful to protein crystals.
About this StructureAbout this Structure
1HJ8 is a Single protein structure of sequence from Salmo salar with SO4, CA and BAM as ligands. Active as Trypsin, with EC number 3.4.21.4 Structure known Active Site: CA1. Full crystallographic information is available from OCA.
ReferenceReference
Atomic resolution structures of trypsin provide insight into structural radiation damage., Leiros HK, McSweeney SM, Smalas AO, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):488-97. PMID:11264577
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