5CKL
Fic protein from Neisseria meningitidis (NmFic) mutant E156R in dimeric form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-02-11 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.8000 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 35.333, 50.538, 130.136 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 65.070 - 0.990 |
| R-factor | 0.1127 |
| Rwork | 0.112 |
| R-free | 0.12460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3s6a |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.200 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.27) |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 65.070 | 65.070 | 1.010 |
| High resolution limit [Å] | 0.990 | 5.420 | 0.990 |
| Rmerge | 0.032 | 0.013 | 0.611 |
| Rpim | 0.013 | 0.006 | 0.258 |
| Total number of observations | 839712 | 5653 | 39446 |
| Number of reflections | 129938 | ||
| <I/σ(I)> | 28.3 | 103.9 | 3.3 |
| Completeness [%] | 99.6 | 99.1 | 97.4 |
| Redundancy | 6.5 | 6.1 | 6.3 |
| CC(1/2) | 1.000 | 1.000 | 0.830 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7.8 | 277.15 | 10 mM Tris pH 7.8, 100 mM NaCl |
