Table 1.
Summary of Crystallographic Information
| Protein | R54E | F403A | K442E |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | P21 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 96.4, 256.7, 127.0 | 96.2, 256.3, 126.7 | 96.6, 258.5, 126.9 |
| α, β, γ (°) | 90, 109.3, 90 | 90, 109.8, 90 | 90, 109.6, 90 |
| Resolution range (Å) a | 30-2.8 (2.9-2.8) | 30-2.8 (2.9-2.8) | 30-3.0 (3.1-3.0) |
| Rmerge (%) | 12.5 (44.7) | 9.2 (46.5) | 6.5 (42.9) |
| I/σI | 10.5 (3.5) | 11.7 (2.1) | 15.5 (2.5) |
| Completeness (%) | 93 (86) | 91 (94) | 98 (99) |
| Redundancy | 4.7 (4.8) | 2.8 (2.8) | 2.8 (2.7) |
| Refinement | |||
| Number of reflections | 125,986 | 122,029 | 109,041 |
| R(%) | 19.4 (26.6) | 20.9 (25.7) | 19.4 (24.5) |
| Rfree (%) | 26.2 (35.2) | 27.9 (35.3) | 26.2 (33.1) |
| Number of atoms | |||
| Protein | 34,009 | 32,422 | 32,401 |
| Ligand | 63 | 62 | 31 |
| Water | 0 | 0 | 0 |
| Average B values (Å2) | |||
| Protein | 26.2 | 49.0 | 40.2 |
| Ligand | 81.6 | 101.1 | 118.8 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.011 | 0.013 | 0.011 |
| Bond angles (°) | 1.3 | 1.4 | 1.2 |
a
The numbers in parentheses are for the highest-resolution shell.