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. Author manuscript; available in PMC: 2011 Aug 11.
Published in final edited form as: Structure. 2010 Aug 11;18(8):934–943. doi: 10.1016/j.str.2010.04.019

Table 2.

Data Collection and Refinement Statistics

Data Collection murine Igβ
monomer
murine Igβ
homodimer
human Igβ
homodimer
Space group P21212 P41212 P4132
Unit cell (Å) a=35.63, b=79.72, c=34.32 a=b=87.97, c=75.29 a=129.83
Resolution limit (Å) 1.7 3.1 3.2
Unique reflections 10471(898)a 5597(541) 6616(630)
Redundancy 5.5(2.3) 6.1(5.4) 27.6(28.7)
Completeness (%) 93.8(67.4) 97.4(98.7) 99.9(100.0)
Rsym (%)b 6.5(31.7) 13.5(50.6) 7.0(33.9)
<I/σ(I)> 21.5(2.6) 14.1(3.2) 55.6(13.1)

Refinement
Resolution (Å) 40.-1.7 48.-3.1 46.-3.2
No. reflections 10071 5407 6407
No. protein atoms 757 1485 1678
No. solvent atoms 92 26 2
Rcryst(%) 18.7(27.0) 20.6(27.8) 18.1(20.7)
Rfree(%)c 19.7(29.0) 25.8(32.0) 26.3(36.2)
Mean B-factor (Å2) 31.7 52.1 77.2
Wilson B-factor (Å2) 20.6 59.7 75.8
r.m.s.d. bond lengths (Å) 0.006 0.007 0.010
r.m.s.d. bond angles (°) 1.18 1.39 1.39
a

Values in parentheses are for highest resolution shells: 1.7-1.74Å, 3.21-3.10Å, and 3.31-3.20Å for murine Igβ monomer, murine Igβ homodimer, and human Igβ homodimer, respectively.

b

Rsym=100×ΣǀIh-<Ih> ǀ/ΣIh, where <Ih> is the mean intensity of multiple measurements of symmetry equivalent reflections.

c

Rfree was calculated using test set of 5%.