Table 1 Data collection and refinement statistics.
From: A distinct holoenzyme organization for two-subunit pyruvate carboxylase
MfPC (B domain of BC deletion, K419A, E421A and E422A mutation) | MfPC (K419A, E421A and E422A mutation) | |
|---|---|---|
Data collection | ||
Space group | R32 | P3121 |
Cell dimensions | ||
a, b, c (Å) | 285.8, 285.8, 274.9 | 160.8, 160.8, 227.7 |
α, β, γ (°) | 90, 90, 120 | 90, 90, 120 |
Resolution (Å) | 50–3.0 (3.1–3.0)* | 50–6.6 (6.83–6.6) |
Rmerge | 8.2 (60.8) | 8.8 (>100) |
CC1/2 | (0.67) | (0.64) |
I/σI | 11.0 (1.8) | 14.9 (1.3) |
Completeness (%) | 96 (96) | 95 (96) |
Redundancy | 2.8 (2.7) | 6.4 (6.3) |
Refinement | ||
Resolution (Å) | 50–3.0 | 50–6.6 |
No. reflections | 77,247 | 6,031 |
Rwork/Rfree | 22.5/27.2 | 27.4/33.4 |
No. of atoms | ||
Protein | 21,658 | 11,277 |
Ligand/ion | 30 | 0 |
Water | 0 | 0 |
B-factors | ||
Protein | 111 | 328 |
Ligand/ion | 77 | — |
Water | — | — |
R.m.s deviations | ||
Bond lengths (Å) | 0.010 | 0.010 |
Bond angles (°) | 1.5 | 1.3 |
