Structural characterization of the mutant BLMs

Copyright information:

Taken from "Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase"

Nucleic Acids Research 2005;33(10):3109-3124.

Published online 1 Jun 2005

PMCID:PMC1142346.

© The Author 2005. Published by Oxford University Press. All rights reserved

() Normalized CD spectra of wild-type and different mutant BLMs (indicated in the figure). The experiments were performed as described under Materials and Methods. About 8 μM of each protein was used in this experiment. All of the spectra are given in units of MRE. () Analysis of wild-type and mutant BLM proteins by size exclusion chromatography. Experiments were performed at room temperature using a Superdex 200 column. Shown are the elution profiles of wild-type and mutant proteins as indicated in the figures. About 5 μM protein was used for each experiment. Insert: The molecular weight calibration to the partition coefficient , using protein molecular weight standards (closed circle), as indicated under Materials and Methods. The open symbols indicate the positions of wild-type and mutants proteins.