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. Author manuscript; available in PMC: 2018 May 2.

Published in final edited form as: Structure. 2017 Apr 13;25(5):762–772.e4. doi: 10.1016/j.str.2017.03.008

Table 1.

X-ray data collection and refinement statistics

	Native_Nsa1_FL	Native_Nsa1_ΔC	SeMet_Nsa1_ΔC
	Data collection

Wavelength (Å)	1.00000	1.00000	0.97911
Space group	P2₁3	P2₁2₁2₁	P2₁2₁2₁
Unit-cell parameters
a, b, c (Å)	a=b=c=163.1	54.3, 81.1, 87.4	54.3, 80.8, 86.7
α, β, γ (°)	α=β=γ=90°	α=β=γ=90°	α=β=γ=90°
Resolution (Å)	50.0 – 2.8 (2.9 – 2.8)^*	59.4–1.3 (1.35 – 1.3)	50.0 – 1.7 (1.76 – 1.7)
R_merge(%)	10.0 (58.4)	6.6 (54.2)	10.1 (81.2)
Mosaicity	0.5	0.3
I/σ(I)	28.9 (5.6)	29.6 (2.3)	19.6 (3.1)
Completeness (%)	96.9 (97.6)	99.9 (99.2)	99.9 (99.7)
Redundancy	10.3 (10.0)	7.2 (6.5)
NO. molecules per ASU	2	1	1
Solvent Content (%)	64.4	33.0	34
Wilson B-factor	47.3	15.7

	Refinement

Resolution (Å)	24.3 – 2.8	59.4 – 1.3
Unique reflections	32680	93271
R_work/R_free (%)	20.4/25.2	12.9/16.2
NO. atoms
Protein	6144	3007
Water	21	440
RMS bonds (Å)	0.015	0.030
RMS angles (°)	1.90	2.43
Ramachandran
Favored (%)	94	96
Allowed (%)	5.9	3.7
Outliers (%)	0.1	0.3
Average B-factor	48.5	22.6

PDB code	5SUM	5SUI

^*

Highest resolution shell are shown in parentheses.