1hj8: Difference between revisions
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|PDB= 1hj8 |SIZE=350|CAPTION= <scene name='initialview01'>1hj8</scene>, resolution 1.00Å | |PDB= 1hj8 |SIZE=350|CAPTION= <scene name='initialview01'>1hj8</scene>, resolution 1.00Å | ||
|SITE= <scene name='pdbsite=CA1:Bam+Binding+Site+For+Residue+A248'>CA1</scene> | |SITE= <scene name='pdbsite=CA1:Bam+Binding+Site+For+Residue+A248'>CA1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BAM:BENZAMIDINE'>BAM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj8 OCA], [http://www.ebi.ac.uk/pdbsum/1hj8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hj8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Mcsweeney, S M.]] | [[Category: Mcsweeney, S M.]] | ||
[[Category: Smalas, A O.]] | [[Category: Smalas, A O.]] | ||
[[Category: atomic resolution]] | [[Category: atomic resolution]] | ||
[[Category: disulphide bond breakage]] | [[Category: disulphide bond breakage]] | ||
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[[Category: trypsin]] | [[Category: trypsin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:06:03 2008'' | ||
Revision as of 21:06, 30 March 2008
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| , resolution 1.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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