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. 2003 Aug;23(16):5638–5650. doi: 10.1128/MCB.23.16.5638-5650.2003

FIG. 5.

FIG. 5.

Protein analyses. (A) Coomassie blue-stained sodium dodecyl sulfate-7.5% polyacrylamide gel of purified proteins. Lane hd, head domain; note that this lane was taken from another gel at its appropriate position relative to the marker. Selected sizes of marker proteins are indicated on the right in kilodaltons. (B) Coomassie blue-stained 7.5% native polyacrylamide gel. Lanes: A, ScpA (2 μM); B, ScpB (10 μM); S, SMC (2 μM); hd, head domain (1.8 μM; this lane was taken from another gel at its appropriate position relative to ScpB and ScpA); other lanes, combinations of A, B, and/or S. Lines at right indicate migration positions for ScpA, ScpB, and the complex (compl); the brace indicates the migration position for SMC. (C) Gel filtration analysis of ScpA, ScpB, and the SMC hinge domain. Standard proteins are indicated by diamonds. (D) Five to 20% sucrose gradient centrifugation of ScpA and ScpB. Migration positions for marker proteins are indicated above the gels.