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

Vadim Rimsa, Thomas Eadsforth, William N. Hunter

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    3 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)442-445
    Number of pages4
    JournalActa Crystallographica F-Structural Biology and Crystallization Communications
    Volume67
    DOIs
    Publication statusPublished - Apr 2011

    Keywords

    • cobalt
    • sentrin-specific protease 1
    • SUMO
    • MAXIMUM-LIKELIHOOD
    • PROSTATE-CANCER
    • PROTEINS
    • BINDING

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