Ab initio protein phasing at 1.4 A resolution

Autor:	Liberato De Caro, Maria Cristina Burla, Giovanni Luca Cascarano, Carmelo Giacovazzo, Benedetta Carrozzini, Giampiero Polidori
Rok vydání:	2003
Předmět:	Diffraction Models Molecular Atomicity Crystallography Computer program Chemistry Direct method Resolution (electron density) Ab initio Proteins Phaser Sensitivity and Specificity Computational science Structural Biology Computational chemistry Lactalbumin Figure of merit Collagen Software phasing
Zdroj:	Acta crystallographica. Section A, Foundations of crystallography 59 (2003): 245–249. doi:10.1107/S0108767303004665 info:cnr-pdr/source/autori:Burla M.C. 1, Carrozzini B. 2, Cascarano G.L. 2, De Caro L. 2, Giacovazzo C. 2, Polidori G. 1/titolo:Ab initio protein phasing at 1.4Å resolution/doi:10.1107%2FS0108767303004665/rivista:Acta crystallographica. Section A, Foundations of crystallography/anno:2003/pagina_da:245/pagina_a:249/intervallo_pagine:245–249/volume:59
ISSN:	0108-7673
Popis:	All the techniques today available for the ab initio crystal structure solution of proteins require that the atomicity condition is satisfied. Accordingly, diffraction data at resolution equal or better than 1.2 A are necessary. This condition reduces the role of the ab initio techniques in macromolecular crystallography. The computer program SIR2002 has been modified in such a way that it may succeed also with 1.4 A resolution diffraction data. The modifications concern all the modules of the program: the modified program also benefits by the efficiency of a figure of merit.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a776a1058a4bd9cccb9a9ced596a6e00 https://pubmed.ncbi.nlm.nih.gov/12714775 Zobrazit plný text záznamu Plný text