Table 1.
Wild-type AphB | N100E AphB | |
---|---|---|
Data collection | ||
Space group | I222 | C121 |
Cell dimensions | ||
a, b, c (Å) | 77.5, 94.6, 59.6 | 268.7, 54.5, 103.8 |
β (°) | 90.0 | 101.0 |
Resolution (Å) | 89.8 -2.2 (2.3-2.2) | 48.1-2.7(2.8-2.7) |
Rmeas | 0.089(0.416) | 0.077(0.472) |
I/σI | 13.1(4.1) | 21.08(4.67) |
Completeness (%) | 99.6 (99.4) | 99.7 (99.4) |
Redundancy | 4.9 (4.9) | 7.4 (7.6) |
Refinement | ||
Resolution (Å) | 48.1-2.2 (2.3-2.2) | 48.1-2.7 (2.8-2.7) |
No. reflections | 49,907 | 39,763 |
Rwork/ Rfree | 0.208/0.234 (0.264/0.305) | 0.201/0.237 (0.271/0.312) |
No. atoms | ||
Protein | 4631 | 9302 |
Water | 349 | 200 |
B-factors | ||
Protein | 48.5 | 53.7 |
Water | 43.8 | 37.8 |
R.m.s deviations | ||
Bond lengths (Å) | 0.008 | 0.002 |
Bond angles (°) | 1.11 | 0.634 |
Highest resolution shell is shown in parenthesis