3SN9
Fic protein from NEISSERIA MENINGITIDIS mutant S182A/E186A in complex with AMPPNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-03 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 110.313, 136.919, 114.663 |
| Unit cell angles | 90.00, 100.26, 90.00 |
Refinement procedure
| Resolution | 15.000 - 3.030 |
| R-factor | 0.222 |
| Rwork | 0.222 |
| R-free | 0.24800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g03 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.114 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (CCP4_3.3.16 2010/01/06) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 87.070 | 87.070 | 3.190 |
| High resolution limit [Å] | 3.020 | 9.560 | 3.020 |
| Rmerge | 0.112 | 0.040 | 0.350 |
| Total number of observations | 8630 | 8487 | |
| Number of reflections | 58488 | ||
| <I/σ(I)> | 6.9449 | 10.48 | 2.17 |
| Completeness [%] | 89.0 | 99.89 | 43.15 |
| Redundancy | 3.8 | 4.01 | 2.06 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 21% PEG3350, 0.2 M di-ammonium tartrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
