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. Author manuscript; available in PMC: 2015 Feb 1.

Published in final edited form as: Nat Struct Mol Biol. 2014 Jun 29;21(8):696–703. doi: 10.1038/nsmb.2846

Table 1.

Data collection and refinement statistics

	Apo-CPB	CPB–Cep192-58mer	CPB–Cep152-60mer
Data collection
Space group	P6₁22	P6₁22	P2₁2₁2
Cell dimensions
a, b, c (Å)	128.1, 128.1, 168.4	67.3, 67.3, 287.6	126.6, 63.9, 79.5
α, β, γ (°)	90.0, 90.0, 120.0	90.0, 90.0, 120.0	90.0, 90.0, 90.0
Resolution (Å)	50.0–2.60 (2.64–2.60)	30.0–2.85 (2.90–2.85)	50.0–2.76 (2.80–2.76)
R_merge	6.8 (27.6)	11.5 (57.4)	6.8 (30.3)
I/σI	48.0 (5.7)	10.9 (3.1)	11.3 (2.6)
Completeness (%)	98.7 (96.7)	99.7 (99.0)	92.0 (71.4)
Redundancy	21.3 (8.5)	9.5 (8.2)	3.8 (2.0)
Refinement
Resolution (Å)	36.1–2.60	29.1–2.85	37.3–2.76
No. reflections	25,386	9,773	15,858
R_work/R_free	0.202/0.249	0.235/0.260	0.258 / 0.288
No. atoms
Protein	3,622	2,033	3,904
Ligand/ion	8	0	0
Water	113	45	16
B factors
Protein	58.3	45.5	50.0
Ligand/ion	74.8	–	–
Water	40.3	38.2	23.4
r.m.s. deviations
Bond lengths (Å)	0.009	0.015	0.004
Bond angles (°)	1.29	1.47	0.92

^*

Values in parentheses are for highest-resolution shell. All diffraction data were obtained from a single crystal.