Combining random microseed matrix screening and the magic triangle for the efficient structure solution of a potential lysin from bacteriophage P68.
Acta Crystallogr D Struct Biol
; 75(Pt 7): 670-681, 2019 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-31282476
ABSTRACT
Two commonly encountered bottlenecks in the structure determination of a protein by X-ray crystallography are screening for conditions that give high-quality crystals and, in the case of novel structures, finding derivatization conditions for experimental phasing. In this study, the phasing molecule 5-amino-2,4,6-triiodoisophthalic acid (I3C) was added to a random microseed matrix screen to generate high-quality crystals derivatized with I3C in a single optimization experiment. I3C, often referred to as the magic triangle, contains an aromatic ring scaffold with three bound I atoms. This approach was applied to efficiently phase the structures of hen egg-white lysozyme and the N-terminal domain of the Orf11 protein from Staphylococcus phage P68 (Orf11 NTD) using SAD phasing. The structure of Orf11 NTD suggests that it may play a role as a virion-associated lysin or endolysin.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Virais
/
Fagos de Staphylococcus
Tipo de estudo:
Clinical_trials
/
Diagnostic_studies
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Prognostic_studies
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Screening_studies
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Austrália