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![[Figure 5]](jb5033fig5mag.jpg)
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Figure 5
Interface analysis of the helical filament structure of the DREP3 CIDE domain. (a) Representative dimeric interface within the helical structure of the DREP3 CIDE domain. The interface formed by molecules 1 (green) and 2 (yellow) was chosen for analysis. (b) Close-up view of the interacting residues in the interface between molecules 1 and 2. The residues involved in the interaction are shown and labelled. Salt bridges formed between one chain and its counterpart are shown as red dashed lines. (c) SEC chromatograms of the wild-type (WT) DREP3 CIDE domain and its mutants. The profile obtained from the WT DREP3 CIDE domain is indicated with a black line, that of the D167R mutant with a blue line and that of the K132D mutant with a red line. All SEC experiments were performed using 20 mM Tris–HCl pH 7.9, 500 mM NaCl buffer. (d) SEC-MALS measurement of the D167R mutant showed the absolute molecular mass of the protein. (e) CD spectra of the WT DREP3 CIDE domain (black line), the D167R mutant (blue line) and the K132D mutant (red line). The spectra were recorded at 25°C and four scans were performed and averaged using a J-715 spectropolarimeter (Jasco, Oklahoma City, Oklahoma, USA). |
![[Figure 5]](jb5033fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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