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![[Figure 2]](ai5014fig2mag.jpg)
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Figure 2
Evaluation of ATAD2B oligomerization. (a) Domain organization of the full-length human ATAD2B protein (amino acids 1–1458) and the GST-tagged, N-terminally truncated ATAD2B expression construct (amino acids 380–1458). For clarity, this GST-ΔN-ATAD2B construct is referred to as ATAD2B throughout the text. (b) 10% SDS–PAGE gel stained with Coomassie Blue showing the molecular-weight (MW) standard and a lane corresponding to the size-exclusion chromatogram peak eluting at ∼9 ml (lane 2). In lane 2, ATAD2B appears as the upper band, migrating above its predicted molecular weight of 150 kDa. Additional bands in the same lane indicate sample heterogeneity. (c) Size-exclusion chromatography traces from a Superdex 200 Increase 10/300 GL column (ÄKTAprime, GE/Cytiva) for the ATAD2B sample (blue) and a MW standard mixture (orange). Monomeric ATAD2B is expected at 150 kDa. The first peak (∼9 ml) elutes near thyroglobulin (670 kDa) consistent with ATAD2B forming an oligomeric complex. The second peak (∼15 ml), eluting before ovalbumin at 44 kDa, corresponds to dimerized GST-tags (∼50 kDa). |
![[Figure 2]](ai5014fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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