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

TY - JOUR

T1 - The role of Co2+in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols

AU - Rimsa, Vadim

AU - Eadsforth, Thomas

AU - Hunter, William N.

PY - 2011/4

Y1 - 2011/4

N2 - 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.

AB - 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.

KW - cobalt

KW - sentrin-specific protease 1

KW - SUMO

KW - MAXIMUM-LIKELIHOOD

KW - PROSTATE-CANCER

KW - PROTEINS

KW - BINDING

U2 - 10.1107/S1744309111005835

DO - 10.1107/S1744309111005835

M3 - Article

SN - 1744-3091

VL - 67

SP - 442

EP - 445

JO - Acta Crystallographica F-Structural Biology and Crystallization Communications

JF - Acta Crystallographica F-Structural Biology and Crystallization Communications

ER -