Table S2.
Data collection and refinement statistics (molecular replacement) for crystal structures of latent AUS1 (natural source and recombinantly expressed)
| Data | Pro-AUS1, natural source | Pro-AUS1, cocrystallized with TEW, recombinantly expressed | Oxy-pro-AUS1, cocrystallized with TEW, recombinantly expressed |
| PDB entry | 4Z11 | 4Z12 | 4Z13 |
| Data collection | |||
| Space group | P1211 | P1211 | P1211 |
| Cell dimensions | |||
| a, b, c, Å | 62.57, 174.1, 102.54 | 52.99, 110.41, 94.99 | 52.88, 109.75, 94.76 |
| α, β, γ, ° | 90.0, 105.3, 90.0 | 90.0, 95.8, 90.0 | 90.0, 96.3, 90.0 |
| Resolution, Å | 46.38–2.50 (2.59–2.50)a | 48.15–1.85 (1.92–1.85) | 47.41–1.78 (1.84–1.78) |
| Rmerge | 0.145 (0.862) | 0.118 (2.729) | 0.112 (1.337) |
| I/σI | 7.6 (2.0) | 8.3 (0.6) | 8.6 (1.0) |
| Number of measured reflections | 242,803 (24,273) | 415,481 (42,647) | 388,959 (38,335) |
| Number of unique reflections | 71,372 (7,074) | 90,863 (8,954) | 101,113 (9,851) |
| Completeness, % | 97.8 (97.7) | 98.1 (97.0) | 98.4 (96.2) |
| Redundancy | 3.4 (3.4) | 4.6 (4.8) | 3.8 (3.9) |
| CC1/2 | 0.986 (0.559) | 0.996 (0.293) | 0.996 (0.453) |
| Refinement | |||
| Resolution, Å | 46.38–2.50 (2.59–2.50)a | 48.15–1.85 (1.92–1.85) | 47.41–1.78 (1.84–1.78) |
| Rwork/Rfree | 0.183/0.234 | 0.172/0.205 | 0.157/0.196 |
| Number of atoms | 16,266 | 8,544 | 8,974 |
| Protein | 15,738 | 7,976 | 8,020 |
| Ligand/ion | 8 | 98 | 96 |
| Water | 520 | 470 | 858 |
| B factors, Å2 | 55.1 | 51.5 | 37.1 |
| Protein | 55.4 | 50.3 | 35.4 |
| Ligand/ion | 49.8 | 153.0 | 114.5 |
| Water | 45.3 | 50.0 | 43.9 |
| rmsd | |||
| Bond lengths, Å | 0.003 | 0.007 | 0.007 |
| Bond angles, ° | 0.66 | 0.99 | 1.02 |
| CC* | 0.996 (0.847) | 0.999 (0.673) | 0.999 (0.790) |
| Ramachandran plot | |||
| Most favored, % | 97.7 | 97.0 | 97.4 |
| Allowed, % | 2.3 | 3.0 | 2.6 |
One crystal was used.
a
Values in parentheses are for highest resolution shell.