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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: Nat Struct Mol Biol. 2014 Nov 2;21(12):1075–1081. doi: 10.1038/nsmb.2907

Table 1.

Summary of Crn1-DCC binding affinities for WT and mutant yeast actins

Kd (µM) Kd/KdWT Coronin residues in close proximity
WT 0.87 ± 0.04 1.00
DNEQ* 0.81 ± 0.01 ~ 1
ΔDSE** 0.76 ± 0.03 ~1
K50A/D51A (red***) 1.55 ± 0.06 ~2 D250 and D273
D80A/D81A (magenta) 1.9 ± 0.5 ~2 R323, K295
E83A/K84A (blue) 5.8 ± 0.3 ~7 K227, D297
E99A/E100A (cyan) 16 ~18 K204, K247
K315A/E316A (green) 1.4 ± 0.1 ~1.6 K20, K21 and E22 (with actin “i+1”)
D363A/E364A (yellow) 4.4 ± 0.8 ~5 R141, R142, and R202 (with actin “i”) R361 and R362 (with actin “i+2”)
R37A/R39A (orange) +Phalloidin **** 2.7 ± 0.1 ~3 E320
WT+150 mM KCl 2.3 ~2–3
*

- D2N/E4Q actin mutant with a neutralized N-terminus.

**

ΔDSE – mutant actin with its three N-terminal residues deleted

***

Color names in parentheses refer to the colors of these residues in Supplementary Fig. 5

****

This set of measurement was carried out in the presence of equimolar concentrations of phalloidin.