The role of Co2+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|67|4|442-445

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.67, Iss.4, 2011-04, pp. : 442-445

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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 Co2+, 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 Co2+ had been overlooked and re‐refinement supported this conclusion. High‐throughput automated re‐refinement protocols also failed to mark the Co2+ position, supporting the requirement for the incorporation of as much information as possible to enhance the value of such protocols.