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![[Figure 1]](jb5071fig1mag.jpg)
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Figure 1
Biochemical characterization of the intended KIF17–IFT70 complex and concealed ArnA contamination. (a) SDS–PAGE analysis of concentrated samples following His-tag affinity purification and SEC. Lanes show purified His-KIF17 alone (left panel) and the reconstituted KIF17–His-IFT70 complex (right panel), allowing direct comparison of band positions with their theoretical molecular weights (MWs). The major bands corresponding to KIF17 and IFT70 were assigned based on this comparative purification under identical conditions. Upon contrast adjustment, an additional faint band migrating near ∼74 kDa can be discerned, consistent with the expected MW of ArnA and comparable to ArnA bands reported previously (see, for example, Shin et al., 2025  ). Apparent MWs in SDS–PAGE deviate slightly from theoretical values, consistent with the elongated and partially disordered nature of KIF17 and IFT70. (b) Mass-spectrometry analysis of the purified sample. Four intermolecular cross-links are indicated by red lines. Cross-linking mass spectrometry confirmed the presence of KIF17 and IFT70 peptides and provided interaction information consistent with complex formation. ArnA peptides were not initially considered during data interpretation but were detected retrospectively upon re-analysis of the dataset. |
![[Figure 1]](jb5071fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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