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. Author manuscript; available in PMC: 2014 Oct 1.
Published in final edited form as: J Struct Biol. 2013 May 30;184(1):21–32. doi: 10.1016/j.jsb.2013.05.014

Table 1.

SAXS data on the various talin polypeptides.

Residues Domains Rg Dmax Angle (SAXS) Angle (EM)
482–786 R1–R2 23.5 71 121 110
655–911 R2–R3 27.4 87 124 128
787–1044 R3–R4 29.7 97 146 145
913–1206 R4–R5 26.9 90 132 139
1046–1357 R5–R6 28.6 105 121 113
1206–1653 R6–R7–R8 31.4 104 116 119
1357–1653 R7–R8 27.8 85 125 111
1357–1822 R7–R8–R9 33.2 110 126 109
1655–1973 R9–R10 27.5 90 129 143
1815–2140 R10–R11 28.1 85.5 124 137
1974–2294 R11–R12 24.7 80 118 109
2137–2482 R12–R13 33.1 120 109 95
2300–2541 R13–DD 37.2 124 n/a n/a

Data obtained from SAXS analysis on the talin polypeptides listed. Rg is the radius of gyration, which gives an indication of the distribution of scattering mass of the polypeptide. Dmax is the maximum linear dimension of the polypeptide. The angle columns give the angle between the long principal axes of the respective domains in the SAXS and EM models respectively.

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