Table 1 Data collection and refinement statistics
From: Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
SeMet-SAD13mergeda | SeMet (5NV9)b | Native (5NVA)c | |
|---|---|---|---|
Data collection | |||
Space group | C2 | C2 | P22121 |
Cell dimensions | |||
a, b, c (Å) | 130.24, 97.99, 54.74 | 130.59, 98.07, 54.78 | 48.78, 97.76, 151.69 |
α, β, γ (°) | 90, 92.16, 90 | 90, 92.15, 90 | 90, 90, 90 |
Resolution (Å)d | 19.93–3.87 (4.32–3.87) | 78.40–1.95 (2.00–1.95) | 82.18–2.26 (2.34–2.26) |
Rsym (%)d | 25.9 (31.7) | 17.4 (134.1) | 14.8 (139.6) |
I/σId | 29.1 (28.6) | 6.43 (1.22) | 8.39 (1.39) |
CC 1/2d | 0.998 (0.997) | 0.991 (0.452) | 0.99 (0.388) |
Completeness (%)d | 99.0 (99.1) | 99.2 (99.6) | 96.64 (95.47) |
Redundancyd | 63.8 (64.4) | 3.24 (3.28) | 4.9 (4.9) |
Refinement | |||
Resolution (Å) | 78.40–1.95 | 82.18–2.26 | |
No. of reflections | 47,316 | 61,303 | |
Rwork/Rfree | 19.88/24.35 | 22.43/26.08 | |
No. of atoms | 3998 | 3834 | |
Protein | 3715 | 3647 | |
Neu5Ac | 21 | 21 | |
Sodium | 2 | 2 | |
DDM | 35 | ||
Phosphate | 5 | ||
Water | 220 | 164 | |
B-factors | 29.9 | 33.9 | |
Protein | 28.5 | 33.6 | |
Neu5Ac | 23.9 | 29.9 | |
Sodium | 27.6 | 32.1 | |
DDM | 47.9 | ||
Phosphate | 54.9 | ||
Water | 42.7 | 42.0 | |
R.m.s. deviations | |||
Bond lengths (Å) | 0.017 | 0.002 | |
Bond angles (°) | 1.85 | 0.51 |
