Figure 2. Homo-oligomerization of β-crystallins. Purified crystallins were incubated for 90 min at either 37 °C or 55 °C and then subjected to SEC-MALS. Eluting proteins were detected by UV absorption at 280 nm (grey line). Molar masses were determined across the peak (solid squares). From molar masses, βB1 was a mixture of monomer-dimers (A); βB2 was predominantly a dimer with less of an earlier eluting peak (B); βA3 WT was a dimer (C); and βA3 DM was a dimer at 37 °C, but had precipitated at 55 °C (D).