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. Author manuscript; available in PMC: 2016 Aug 1.
Published in final edited form as: J Struct Biol. 2015 Jun 4;191(2):236–244. doi: 10.1016/j.jsb.2015.06.003

Table 1.

Data collection and refinement statistics.

EspB7-278
(PDB: 4XWP)
EspB7-278
(PDB: 4XXX)
EspB7-278
(PDB: 4XXN)
EspB1-460
(PDB: 4XY3)
Data collection
Space group C2221 C2221 I222 C2221
Cell dimensions □□
a, b, c (Å) 66.24, 69.51,
119.14
67.34, 69.58, 119.60 73.12, 93.07,
142.94
72.11, 146.49,
94.22
 α□ β□ γ□ (°) 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90
Resolution (Å) 59.6–1.82 (1.92–
2.00)1
59.8–1.50 (1.58–
1.50)
71.5–2.14 (2.26–
2.14)
47.11–3.04 (3.20–
3.04)
R sym 0.060 (0.945) 0.047 (0.747) 0.092 (0.873) 0.135 (0.917)
CC1/22 99.9 (86.3) 100.0 (88.4) 99.7 (54.1)
I / σI 17.8 (2.4) 18.6 (2.0) 13.8 (2.83) 9.0 (1.73)
Completeness (%) 100.0 (100.0) 99.7 (98.3) 97.8 (98.7) 95.7 (97.5)
Multiplicity 6.9 (7.0) 5.4 (5.1) 5.4 (5.5) 5.1 (5.1)
Refinement
Resolution (Å) 59.6–1.82 59.8–1.50 71.5–2.14 47.11–3.04
No. reflections (total /
free)
25047 / 1264 44892 / 2191 26733 / 1385 9490 / 491
Rwork / Rfree 0.199 / 0.234 0.194 / 0.218 0.204 / 0.251 0.220 / 0.266
No. atoms
 Protein 1863 1972 1875 1903
 Ligand/ion 1 13 2 0
 Water 159 263 174 0
B-factors
 Protein 37.6 27.2 45.6 82.5
 Ligand/ion 56.8 36.0 50.8
 Water 43.4 36.5 46.6
 Wilson B 37.2 27.6 40.8 63.0
R.m.s. deviations
 Bond lengths (Å) 0.009 0.014 0.010 0.008
 Bond angles (°) 1.228 1.518 1.312 1.220
Ramachandran
distribution (%)3
 Favored 100.0 100.0 98.7 94.6
 Outliers 0.0 0.0 0.0 0.8
1

Values in parentheses are for the highest-resolution shell.

2

Half-set correlation coefficient CC1/2 as defined in Karplus and Diederichs (Karplus and Diederichs, 2012) and calculated using XSCALE (Kabsch, 2010) or Scala (Evans, 2006).

3

Calculated using the MolProbity server (http://molprobity.biochem.duke.edu) (Chen et al., 2010).