Skip to main content
. Author manuscript; available in PMC: 2015 Feb 6.
Published in final edited form as: Mol Cell. 2014 Feb 6;53(3):498–505. doi: 10.1016/j.molcel.2014.01.010

Figure 1. Structure of the Swr1589-650-scH2B-H2A.Z complex.

Figure 1

(A) Illustration of the location of the ATPase domains and the amino acid sequence in the region 599–627 of the Swr1 subunit. The letters in bold indicate the amino acids that are folded in the complex, whereas the regular letters indicate the disordered loop.

(B) Deviation of Cα chemical shifts of Swr1589-650 from random coil values: Swr1589-650 in the free form (upper panel) and in complex with scH2B-H2A.Z (lower panel). The regions in red are not observable because they form folded structures in the complex and the complex is larger than 25 kDa.

(C) Velocity sedimentation result of the Swr1589-650-scH2B-H2A.Z complex, showing a S20,w of 2.54S complex with a molecular weight of 27.7 kDa.

(D) Overall structure of the Swr1589-638-scH2B-H2A.Z complex. Only regions 599–605 and 614–627 in the Swr1-Z domain are folded in the complex. See also Figure S1.