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![[Figure 3]](jb5070fig3mag.jpg)
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Figure 3
Oligomeric state and interfacial analysis of Fsc1. (a) Size-exclusion chromatography (SEC) profile of purified Fsc1 showing a predominant dimeric species (∼145 kDa). The corresponding molecular weights (in kDa) are indicated on both the chromatogram and the SDS–PAGE gel. (b) Denaturing SDS–PAGE and blue native PAGE of the Fsc1 construct. Bovine serum albumin (BSA) was included as a marker for the native gel run. (c) Dimer interface in crystal form A, with key residues involved in hydrogen bonding and salt-bridge formation highlighted. (d) Dimer interface in crystal form B, showing similar interactions to (c), with the key residues highlighted. (e) Surface properties of the Fsc1 dimerization interface. One protomer (dark blue) is shown with interface residues colored by chemical property: hydrophilic (yellow) and hydrophobic (orange). (f) Representative electron density at the dimer interface. The 2Fo − Fc map (contoured at 1.5σ) shows well defined density for polar side chains involved in the interactions. (g) Superimposition of the dimer interfaces from both crystal forms, as depicted in (c) and (d), reveals a consistent topology that supports biological relevance. |
![[Figure 3]](jb5070fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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