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. Author manuscript; available in PMC: 2012 Jan 14.
Published in final edited form as: J Mol Biol. 2010 Nov 12;405(2):479–496. doi: 10.1016/j.jmb.2010.11.007

Table 1.

Summary of diffraction data and refinement statistics

Space group P21
Unit cell dimensions a = 60.2 Å, b = 90.4 Å, c = 70.6 Å,
β = 111°
Subunits per asymmetric unit 2
Resolution range (Å)a 27-1.73 (1.77-1.73)
Rmerge b 0.069 (0.517)
Completeness (%) 95 (98)
cRcryst 0.19 (0.26)
cRfree 0.24 (0.29)
RMSD bond lengths (Å) / RMSD bond
angles (°)
0.005/0.856
No. protein atoms 5562
Wilson / Mean protein B-factor (Å2)
(isotropic equivalent)
17.6 / 26.7
Estimated error (Max. likelihood, Å) 0.23
a

Numbers in parentheses are values in highest resolution shell

b

Rmerge = Σhkl Σi | Ii(hkl) - <I(hkl)>|/Σhkl Σi Ii(hkl), where Ii(hkl) is the ith observation of a symmetry equivalent of reflection hkl.