1ayp
From Proteopedia
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[[Image:1ayp.gif|left|200px]] | [[Image:1ayp.gif|left|200px]] | ||
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'''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT''' | '''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT''' | ||
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A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299314 15299314] | A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299314 15299314] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:51:24 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:51, 2 May 2008
A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT
Overview
It is often found in the crystallization of enzyme-inhibitor complexes that an inhibitor causes crystal packing which is different to that of native protein. This is the case for crystals of human non-pancreatic secreted phospholipase A(2) (124 residues) containing six molecules in the asymmetric unit when the protein is complexed with a potential acylamino analogue of a phospholid. The hexameric structure was determined by molecular replacement using the structure of monomeric native protein as a probe. As an extension to the experiment, it was tested whether a backbone polypeptide composed of 17% of a known monomeric structure could find its correct position on a target molecule in molecular replacement. A probe model composed of the backbone atoms of the N-terminal 77 residues of lysine-, arginine-, ornithine-binding protein (LAO, a total of 238 residues) liganded with lysine correctly finds its position on LAO liganded with histidine which crystallizes as a monomer in the asymmetric unit. The results indicate that as little as 17% of total diffracting matter can be used in molecular replacement to solve crystal structures or to obtain phase information which can be combined with phases obtained by the isomorphous-replacement method.
About this Structure
1AYP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:15299314 Page seeded by OCA on Fri May 2 10:51:24 2008
