Table 1 Data collection, phasing and refinement statistics.
From: Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
TEX12 ΔCtip | TEX12 FFV dimer | TEX12 FFV helical | |
|---|---|---|---|
PDB accession | 6HK8 | 6HK9 | 6R2F |
Data collection | |||
Space group | P6522 | C2221 | I212121 |
Cell dimensions | |||
a, b, c (Å) | 47.97, 47.97, 210.98 | 43.23, 219.71, 37.50 | 59.86, 104.51, 127.51 |
α, β, γ (°) | 90.00, 90.00, 120.00 | 90.00, 90.00, 90.00 | 90, 90, 90 |
Resolution (Å) | 52.75–2.11 (2.15–2.11)a | 54.93–1.45 (1.48–1.45)a | 40.41–2.29 (2.37–2.29)a |
Rmeas | 0.082 (2.330) | 0.044 (0.472) | 0.144 (1.511) |
Rpim | 0.014 (0.374) | 0.017 (0.170) | 0.073 (0.756) |
I / σ(I) | 28.1 (2.4) | 20.3 (2.6) | 8.7 (1.6) |
CC1/2 | 1.000 (0.890) | 0.999 (0.993) | 0.998 (0.708) |
Completeness (%) | 92.7 (100.0) | 98.1 (96.6) | 99.6 (99.2) |
Redundancy | 34.5 (37.5) | 7.1 (7.4) | 7.2 (7.4) |
Refinement | |||
Resolution (Å) | 41.54–2.11 | 30.97–1.45 | 40.41–2.29 |
UCLA anisotropy (Å) | 2.2, 2.2, 2.1 | N/A | N/A |
No. reflections | 7701 | 59176 | 18283 |
Rwork/Rfree | 0.2291/0.2580 | 0.1795/0.2047 | 0.2378/0.2621 |
No. atoms | 1146 | 1536 | 2226 |
Protein | 1056 | 1313 | 1991 |
Ligand/ion | 30 | 23 | 90 |
Water | 60 | 200 | 145 |
B-factors | 55.63 | 37.67 | 54.76 |
Protein | 54.99 | 35.55 | 54.00 |
Ligand/ion | 73.83 | 59.85 | 60.82 |
Water | 57.82 | 49.06 | 61.4 |
R.m.s. deviations | |||
Bond lengths (Å) | 0.002 | 0.008 | 0.007 |
Bond angles (°) | 0.316 | 0.856 | 0.941 |
