1n6y: Difference between revisions
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|PDB= 1n6y |SIZE=350|CAPTION= <scene name='initialview01'>1n6y</scene>, resolution 1.40Å | |PDB= 1n6y |SIZE=350|CAPTION= <scene name='initialview01'>1n6y</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ABN:BENZYLAMINE'>ABN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=[[1n6x|1N6X]], [[1n7a|1N7A]], [[1n7b|1N7B]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6y OCA], [http://www.ebi.ac.uk/pdbsum/1n6y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n6y RCSB]</span> | |||
}} | }} | ||
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[[Category: Pan, B.]] | [[Category: Pan, B.]] | ||
[[Category: Ravelli, R B.G.]] | [[Category: Ravelli, R B.G.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''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 22:26:15 2008'' | ||
Revision as of 22:26, 30 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Related: | 1N6X, 1N7A, 1N7B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIP-phasing on Bovine Trypsin
OverviewOverview
The use of third generation synchrotron sources has led to renewed concern about the effect of ionizing radiation on crystalline biological samples. In general, the problem is seen as one to be avoided. However, in this paper, it is shown that, far from being a hindrance to successful structure determination, radiation damage provides an opportunity for phasing macromolecular structures. This is successfully demonstrated for both a protein and an oligonucleotide, by way of which complete models were built automatically. The possibility that, through the exploitation of radiation damage, the phase problem could become less of a barrier to macromolecular crystal structure determination is discussed.
About this StructureAbout this Structure
1N6Y is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Specific radiation damage can be used to solve macromolecular crystal structures., Ravelli RB, Leiros HK, Pan B, Caffrey M, McSweeney S, Structure. 2003 Feb;11(2):217-24. PMID:12575941
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