The role of Co²+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 4): 442-5, 2011 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-21505236
ABSTRACT
Metal ions often stabilize intermolecular contacts between macromolecules, thereby promoting crystallization. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation was noted. This was assigned as Co(2+), an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggested that Co(2+) had been overlooked and re-refinement supported this conclusion. High-throughput automated re-refinement protocols also failed to mark the Co(2+) position, supporting the requirement for the incorporation of as much information as possible to enhance the value of such protocols.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Cobalto
/
Cristalografia por Raios X
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Reino Unido