. Author manuscript; available in PMC: 2013 Sep 1.

Published in final edited form as: Nat Struct Mol Biol. 2013 Feb 3;20(3):355–362. doi: 10.1038/nsmb.2497

Table 1.

Data collection and refinement statistics

	Gα_q–PLCβ3
Data collection
Space group	P2₁2₁2₁
Cell dimensions
a, b, c (Å)	91.2, 190, 291
α, β, γ (°)	90, 90, 90
Resolution (Å)	20.0–4.00 (4.07–4.00)^*
R_merge	0.14 (0.33)
I / σI	8.8 (1.9)
Completeness (%)	76.7 (36.7)
Redundancy	3.3 (2.1)
Refinement
Resolution (Å)	20.0–4.0
No. reflections	32,433
R_work / R_free	0.214/0.255
No. atoms
Protein	39,306
Ligand/ion	98
B-factors (Å²)
Protein	136
Ligand/ion	100
R.m.s. deviations
Bond lengths (Å)	0.005
Bond angles (°)	0.86

Values in parentheses are for highest-resolution shell. Data sets collected from multiple regions of two crystals were merged, and a σ cutoff of 0 was applied during scaling to help limit the effects of radiation damage that occurred over each sweep of data. The data was 85.6% complete at 6.8 Å resolution. Before applying the σ cutoff, there were 41,201 total reflections, corresponding to 91.1% overall completeness.