Extending molecular-replacement solutions with SHELXE

Although the program SHELXE was originally intended for the experimental phasing of macromolecules, it can also prove useful for expanding a small protein fragment to an almost complete polyalanine trace of the structure, given a favourable combination of native data resolution (better than about 2....

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Detalles Bibliográficos
Autores principales: Thorn, Andrea, Sheldrick, George M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3817699/
https://www.ncbi.nlm.nih.gov/pubmed/24189237
http://dx.doi.org/10.1107/S0907444913027534
Descripción
Sumario:Although the program SHELXE was originally intended for the experimental phasing of macromolecules, it can also prove useful for expanding a small protein fragment to an almost complete polyalanine trace of the structure, given a favourable combination of native data resolution (better than about 2.1 Å) and solvent content. A correlation coefficient (CC) of more than 25% between the native structure factors and those calculated from the polyalanine trace appears to be a reliable indicator of success and has already been exploited in a number of pipelines. Here, a more detailed account of this usage of SHELXE for molecular-replacement solutions is given.

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