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. Author manuscript; available in PMC: 2012 Feb 21.
Published in final edited form as: J Immunol. 2011 Aug 19;187(6):3208–3217. doi: 10.4049/jimmunol.1101467

Table I.

Summary of data collection and crystallographic refinements

FcγRIIa-LR FcγRIIa-HR FcγRIIa-HR–Fc
Data collection
    Space group P21212 C2221 C2221
    Cell dimensions
    a, b, c (Å) 79.34, 100.41, 27.94 50.04, 77.94, 88.10 153.38, 255.55, 58.44
    Resolution (Å) 20–1.5 (1.55–1.5)a 30–2.3 (2.38–2.3) 30–3.8 (3.94–3.8)
    Rsym 0.052 (0.32) 0.10 (0.27) 0.14 (0.35)
    Mean I/σ(I)a 21.8 (3.8) 13.2 (4.9) 10.8 (3.78)
    Completeness (%) 94.5 (85.5) 97.2 (96.0) 98.9 (99.7)
    Redundancy 6.1 (4.0) 4.6 (4.3) 5.0 (4.8)
Refinement
    Resolution (Å) 19.8–1.5 20.4–2.3 29.7–3.8
    No. of reflections 34,590 7,554 11,110
    Rwork/Rfree 0.20/0.23 0.21/0.28 0.25/0.42
    No. of atoms
    Protein 1,354 1,350 4,745
    Ligand 14 0 376
    Water 273 85 24
    B-factors
    Protein 22.7 20.7 34.5
    Water 36.5 23.1 26.6
    RMSD bond lengths (Å) 0.005 0.006 0.010
    RMSD bond angles (°) 1.3 1.4 1.8
a

Values in parentheses are for the highest resolution shell.

RMSD, root-mean-square deviation.