Skip to main content
. 2019 Aug 9;28(10):1819–1829. doi: 10.1002/pro.3696

Table 1.

X‐ray crystallographic data and refinement statistics for Fstl1‐FK

Data collection
Space group P6 2
Wavelength (å) 1.5418
Unit cell dimensions
a (å) 45.73
b (å) 45.73
c (å) 68.97
α, β, γ (°) 90, 90, 120
Molecules per ASUa 1
Resolution (å)b 30–2.3 (2.37–2.30)
Completeness (%)b 99.89 (99.98)
Redundancyb 9.95 (8.14)
No. of total reflectionsb 36,506 (3,785)
No. of unique reflectionsb 3,669 (465)
I/σ b 25.3 (2.5)
R sym b , c 5.2 (35.3)
Refinement statistics
Resolution (å) 2.30
No. of reflections 3,669
R work/R free (%)d , e 20.20/23.57
No. of atoms
Protein 652
Water 34
B‐factors (å2)
Protein 49.11
Water 40.77
R.m.s. deviations
Bond length (å) 0.010
Bond angle (°) 1.253
Ramachandran analysis
Favored (%) 96.20
Allowed (%) 3.80
Outliers (%) 0
a

ASU, asymmetric unit.

b

Values in parentheses are for the highest resolution shell.

c

R sym = ∑|I − <I>|/∑<I>, where I is the observed intensity, and <I> is the average intensity of multiple observations of symmetry related reflections.

d

R = ∑hkl||F obs| − |F calc||/∑hkl|F obs|.

e

R free is calculated from 5% of the reflections excluded from refinement.