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. Author manuscript; available in PMC: 2016 Nov 19.
Published in final edited form as: Biochemistry. 2016 Jul 22;55(30):4239–4253. doi: 10.1021/acs.biochem.6b00246

Table 1.

X-ray diffraction data collection and refinement statisticsa

Data collection
Wavelength (Å) 0.97921
Data range (Å) 40.15–1.46
Space group C2
Unit Cell a=58.20 Å,
b=71.58 Å,
c=58.45 Å,
β=112.55°
Unique reflections 38596 (3766)
Avg. multiplicity 7.5 (7.1)
Mosaicity 0.21
Completeness (%) 99.70 (97.97)
CC1/2 0.98 (0.86)
1 Rmeas 0.11 (0.70)
I/σI 15.91 (2.99)
Refinement
Model:
Chain A (number of residues) 93
Chain B (number of residues) 93
Water molecules 255
Data Range (Å) 40.15–1.46
2Rwork (%) 17.2
2,3Rfree (%) 20.8
Average B-values (Å2):
Main Chain 22.8
Side Chain 37.6
Water 43.0
All Atoms 32.3
RMSDs from target values:
Bond Lengths (Å) 0.007
Bond Angles (°) 0.71
Ramachandran outliers 0

Values in parentheses pertain to the highest resolution shell.

1

Rmeas = Σhkl (n/n−1)1/2 Σh,i |Ihkl,i−<Ihkkl>|/ΣhklΣh,iIhkl,i.

2

R factor= Σh, |Fobs−|Fcalc|/Σh|Fobs|.

3

Test set for Rfree consisted of 5.0 % of data.