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. 2015 Jun 27;71(Pt 7):870–875. doi: 10.1107/S2053230X15005956

Figure 2.

Figure 2

Characterization of the AtBAG5 (49–153)–CaM complex. (a) SDS–PAGE analysis of the final purity of AtBAG5 (49–153) and CaM. The gel was stained with Coomassie Brilliant Blue R-250. Lane 1, molecular-mass marker (labelled in kDa); lane 2, purified AtBAG5 (49–153); lane 3, purified CaM in the buffer containing 5 mM EGTA. For this gel, 10 µg AtBAG5 (49–153) and 20 µg CaM were loaded. (b) Gel-filtration profiles of the AtBAG5 (49–153)–CaM complex, CaM alone and AtBAG5 (49–153) alone using the same HiLoad 26/60 Superdex 200 size-exclusion column. (c) SDS–PAGE analysis of the major elution peak corresponding to the AtBAG5 (49–153)–CaM complex eluted from gel filtration. The gel was stained with Coomassie Brilliant Blue R-250. Lane 1, molecular-mass marker (labelled in kDa); lane 2, protein samples mixed in a molar ratio of 1:1 as loaded onto the gel-filtration column; lanes 3–10, fraction samples corresponding to the major elution peak of the protein complex.