Table 1 Data collection and refinement statistics.

From: Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Space group citrate bound Atg18 phosphate bound Atg18
P1 P1
cell dimensions
a, b, c (Å) 57.8, 58.0, 62.2 58.2, 58.3, 62.3
α, β, γ (°) 84.2, 81.2, 87.0 83.7, 80.9, 86.8
resolution (highest res. shell) (Å) 41.3–2.0 (2.1–2.0) 45.5–2.5 (2.7–2.5)
Rfactor (%) 5.7 (36.1) 13.3 (64.5)
wavelength (Å) 1.000 0.979
no. of observed reflections/unique reflections 102367/51797 200927/27376
I/σ (I) 9.6 (2.2) 12.8 (3.4)
completeness (%) 94.5 (86.3) 98.3 (96.5)
Wilson B factor (Å2) 32.1 41.2
Refinement
molecules per unit cell 2 2
Rwork/Rfree (%) 21.4/26.9 22.1/26.5
residues included in model A: 32–179, 201–296, 438–467, 485–524 A:33–179, 201–297, 438–467, 484–424
B: 32–180, 201–297, 438–467, 484–525 B: 33–179, 201–297, 438–467, 485–525
number of protein atoms 4835 4751
number of ligand atoms 36 24
number of water molecules 385 119
B-factors (Å 2) overall 29.0 39.4
protein 28.5 39.4
ligand 42.3 49.2
water 33.7 35.0
r.m.s.d.
bond lengths (Å) 0.010 0.003
bond angles (°) 1.20 0.65
Ramachandran favored/allowed/outliers (%) 97.4/2.4/0.2 96.6/3.4/0