Skip to main content

View full-text article in PMC

. Author manuscript; available in PMC: 2012 Mar 1.

Published in final edited form as: Nat Struct Mol Biol. 2011 Aug 7;18(9):999–1005. doi: 10.1038/nsmb.2095

Table 1.

Data collection and refinement statistics

	Sepia PLC21	Loligo PLC21
Data collection
Space group	P2₁2₁2₁	P2₁2₁2₁
Cell dimensions
a, b, c (Å)	60.8, 83.4, 163.1	82.4, 148.9, 151.6
α, β, γ (°)	90, 90, 90	90, 90, 90
Resolution (Å)	27.4-2.00 (2.04-2.00)^*	29.97-3.10 (3.15-3.10)
R_sym or R_merge	0.069 (0.679)	0.146 (0.814)
I / σI	17.4 (1.58)	14.2 (2.3)
Completeness (%)	97.7 (98.2)	100 (100)
Redundancy	3.7 (3.6)	7.2 (7.2)
Refinement
Resolution (Å)	27.4-2.00	30.0-3.20
No. reflections	53335	29832
R_work / R_free	0.176/0.208	0.232/0.256
No. atoms
Protein	12668	24953
Ligand/ion	126	2
Water	452	38
B-factors
Protein	20.2	61.5
Ligand/ion	45.9	60.2
Water	28.1	36.3
R.m.s. deviations
Bond lengths (Å)	0.006	0.006
Bond angles (°)	0.946	0.881

Each data set was collected from a single crystal.

^*

Values in parentheses are for highest-resolution shell.