1n6y: Difference between revisions

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New page: left|200px<br /><applet load="1n6y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6y, resolution 1.40Å" /> '''RIP-phasing on Bovin...
 
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[[Image:1n6y.jpg|left|200px]]<br /><applet load="1n6y" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1n6y.jpg|left|200px]]<br /><applet load="1n6y" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1n6y, resolution 1.40&Aring;" />
caption="1n6y, resolution 1.40&Aring;" />
'''RIP-phasing on Bovine Trypsin'''<br />
'''RIP-phasing on Bovine Trypsin'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1N6Y 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 SO4, CA, ABN and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N6Y OCA].  
1N6Y 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=SO4:'>SO4</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ABN:'>ABN</scene> and <scene name='pdbligand=GOL:'>GOL</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=1N6Y OCA].  


==Reference==
==Reference==
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[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Caffrey, M.]]
[[Category: Caffrey, M.]]
[[Category: Leiros, H.K.S]]
[[Category: Leiros, H K.S]]
[[Category: McSweeney, S.]]
[[Category: McSweeney, S.]]
[[Category: Pan, B.]]
[[Category: Pan, B.]]
[[Category: Ravelli, R.B.G.]]
[[Category: Ravelli, R B.G.]]
[[Category: ABN]]
[[Category: ABN]]
[[Category: CA]]
[[Category: CA]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:00:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:53 2008''

Revision as of 15:02, 21 February 2008

File:1n6y.jpg


1n6y, resolution 1.40Å

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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 with , , and as ligands. Active as Trypsin, with EC number 3.4.21.4 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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