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![[Figure 1]](jn0084fig1mag.jpg)
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Figure 1
Elution profiles of gel-filtration runs performed with eEF1Bα and the eEF1A–eEF1Bα complex on a Superdex 200 HR gel-filtration column. The molecular weights of the proteins used to calibrate the column are 150 (left), 66 (middle) and 12.6 kDa (right) and are indicated with arrows. (a) eEF1Bα digested with trypsin elutes in three peaks, with the C-terminal fragment in peak 2 eluting at 30 kDa. Peak 1, eluting at 50 kDa, represents partially aggregated digested eEF1Bα, while peak 3 represents small peptides from the trypsin degradation. (b) The elution profile of eEF1A in complex with the eEF1Bα C-terminal fragment displays two peaks corresponding to the eEF1A–eEF1Bα complex, eluting at 62 kDa, and a surplus of eEF1Bα fragment, eluting at 30 kDa. The apparent molecular weight of 30 kDa for the eEF1bα fragment may indicate dimer formation, but it may also be explained by its highly elongated shape (Andersen et al., 2000  ). |
![[Figure 1]](jn0084fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
