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Template convolution to enhance or detect structural features in macromolecular electron-density maps
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
1997 (English)In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, ISSN 0907-4449, Vol. 53, 179-185 p.Article in journal (Refereed) Published
Abstract [en]

A conceptually simple real-space convolution method has been developed which can be used to detect or enhance structural features in experimental macromolecular electron-density maps. The method has been implemented in a computer program (ESSENS). One application of the method is in selectively visualizing secondary-structure elements in multiple isomorphous replacement (MIR) maps of proteins, prior to map interpretation. This application is demonstrated for MIR maps of P2 myelin protein [Jones, Bergfors, Sedzik & Unge (1988). EMBO J. 7, 1597-1604; Cowan, Newcomer & Jones (1993). J. Mol. Biol. 230, 1225-1246] and glyoxalase I [Cameron, Olin, Ridderstrom, Mannervik & Jones (1997). In preparation]. Another application is in finding the optimal orientation and position of a known structural fragment (e.g. a protein domain or a ligand) in any type of electron-density map (real-space or phased molecular replacement). This application is demonstrated for the complex of acetylcholinesterase and the snake toxin fasciculin II [Harel, Kleywegt, Ravelli, Silman & Sussman (1995). Structure, 3, 1355-1366] where the toxin was located in a map phased using the molecular-replacement solution for the acetylcholinesterase alone.

Place, publisher, year, edition, pages
1997. Vol. 53, 179-185 p.
Keyword [en]
P2 MYELIN PROTEIN; REFINEMENT
Identifiers
URN: urn:nbn:se:uu:diva-79646OAI: oai:DiVA.org:uu-79646DiVA: diva2:107559
Available from: 2006-12-15 Created: 2006-12-15 Last updated: 2011-01-15

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