SIR2000, a program for the automatic ab initio crystal structure solution of proteins

Autor:	Carmelo Giacovazzo, Mercedes Camalli, Maria Cristina Burla, Riccardo Spagna, Benedetta Carrozzini, Giovanni Luca Cascarano, Giampiero Polidori
Jazyk:	angličtina
Rok vydání:	2000
Předmět:	Diffraction Crystallography Chemistry Direct method Resolution (electron density) Ab initio Proteins Crystal structure protein solution Phaser Enzymes Solutions Data flow diagram Reciprocal lattice Structural Biology Computational chemistry computer program Algorithm Software
Zdroj:	Acta crystallographica. Section A, Foundations of crystallography 56 (2000): 451–457. doi:10.1107/S0108767300006966 info:cnr-pdr/source/autori:BURLA M.C. 2; CAMALLI M 3; CARROZZINI B 4; CASCARANO GL 4 ; GIACOVAZZO C 1,4; POLIDORI G 2 & SPAGNA R 3/titolo:SIR2000, a program for the automatic ab initio crystal structure solution of proteins/doi:10.1107%2FS0108767300006966/rivista:Acta crystallographica. Section A, Foundations of crystallography/anno:2000/pagina_da:451/pagina_a:457/intervallo_pagine:451–457/volume:56
DOI:	10.1107/S0108767300006966
Popis:	A new phasing procedure is described working both in direct and in reciprocal space. The procedure has been implemented into the program SIR2000, the heir to SIR99, and it is able routinely to solve ab initio crystal structures of proteins without any use of prior information and any user intervention. The moduli and the flow diagram of SIR2000 are also described and its efficiency tested on several protein diffraction data sets. Success has been attained for crystal structures with up to almost 2000 non-hydrogen atoms in the asymmetric unit and resolution higher than 1.2 A. The phasing process is analysed to provide a better insight into the role of the various steps of the procedure.
Databáze:	OpenAIRE
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