. 2014 Mar 26;9(3):e93156. doi: 10.1371/journal.pone.0093156

Table 1. Statistics on data collection, phasing, and refinements of CBA120 TSP1 structure.

Data Collection
	Se-Met TSP1				Wild-type TSP1
	Peak^b	Inflection^b	High Remote^b	Low Remote^c
Wavelength (Å)	0.97945	0.97961	0.94945	1.03320	1.03320
Space Group	P2₁2₁2₁
Cell Dimension (Å)	123.23, 153.09, 171.44				123.61, 147.82, 170.63
^aResolution (Å)	20–2.2 (2.26–2.2)	20–2.2 (2.26–2.2)	20–2.2 (2.26–2.2)	90–1.8 (1.85–1.8)	73.9–1.8 (1.85–1.8)
^aCompleteness (%)	99.0 (96.3)	98.7 (95.1)	98.9 (95.7)	99.6 (99.1)	99.8(99.6)
No. of unique Reflections	316917	317685	317478	297461	298512
^aRedundancy	3.4 (2.6)	3.4 (2.6)	3.4 (2.6)	6.5 (4.2)	6.7 (4.9)
^a R _merge	0.087 (0.363)	0.096 (0.448)	0.095 (0.413)	0.087 (0.500)	0.094 (0.510)
^a I/σ(I)	10.3 (2.6)	9.4 (2.0)	9.6 (2.2)	13.3 (2.1)	11.9 (2.2)
MAD-Phasing
^aResolution	20–2.3 (2.41–2.30)
No. of Se atoms (found/correct)	32/29
^aInitial figure of merit (FOM)	0.46 (0.27)
^aFOM after density modification	0.67 (0.32)
Refinement
	Se-Met TSP1				Wild-type TSP1
^aResolution (Å)	90–1.8 (1.82–1.8)				63.4–1.8 (1.85–1.8)
^a R _work	0.187 (0.369)				0.189 (0.375)
^a R _free	0.204 (0.384)				0.207 (0.398)
RMSD bond length (Å)/bond angle (°)	0.008/1.1				0.007/1.4
Ramachandran plot: Favored/Allowed/Disallowed (%)	86.6/13.2/0.2				87.0/12.9/0.1
No. of protein atoms	16865				16972
No. of Zn²⁺ ion	1				1
No. of water molecules	2361				2449

The values in parentheses are for the highest resolution shell.

R _merge = Σ_hkl [(Σ_j|I_j−<I>|)/Σ_j|I_j|].

R _work = Σ_hkl| |F_o|−|F_c| |/Σ_hkl|F_o|, where F_o and F_c are the observed and calculated structure factors, respectively.

R _free is computed from 5% randomly selected reflections that were omitted from the refinement.

data processed with anomalous signal.

data processed without anomalous signal (for refinement only).