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. Author manuscript; available in PMC: 2012 Jun 8.
Published in final edited form as: Biochemistry. 2010 Dec 8;50(1):93–105. doi: 10.1021/bi101288y

Table 1.

Crystallographic data-collection and refinement statistics for hRXRα-LBD:9cRA:GRIP-1 complex*

Unit Cell parameters (Å, °) a=65.83, b=65.83, c=1 11.86
α=90, β=90, γ=90
Space group P43212
Resolution (last shell) (Å) 50–2.05 (2.12–2.05)
No. of total/unique reflections 229000/16156
Rmerge (last shell) (%) 0.071 (0.324)
Redundancy (last shell) 14.2 (14.1)
Completeness (last shell) (%) 100.0 (99.9)
I/sigma (last shell) 13.2 (9.3)
Refinement
No. of Residues 213
No. of protein atoms 1791
No. of water molecules 144
No. of ligand atoms 22
Rcryst (%) 20.5
Rfree (%) 24.2
R.M.S. Deviation from ideality
Bond length (Å) 0.0057
Bond angles (°) 1.135
Ramachandran plot, residues in Most favored regions (%) 94.98
Additional allowed regions (%) 3.20
Generously allowed regions (%) 1.82
Average B factor (Å2) 30.85
Nonhydrogen protein atoms (Å2) 29.78
Nonhydrogen ligand atoms (Å2) 39.79
Water molecules (Å2) 37.72