4Z3T
Meningococcal Factor H binding protein mutant L130R/G133D
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.977 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.549, 35.670, 90.410 |
| Unit cell angles | 90.00, 104.11, 90.00 |
Refinement procedure
| Resolution | 66.025 - 1.620 |
| R-factor | 0.1954 |
| Rwork | 0.194 |
| R-free | 0.23070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | homology model from 3KVD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.042 |
| Data reduction software | iMOSFLM (1.0) |
| Data scaling software | SCALA (CCP4 v.6.4.0) |
| Phasing software | MOLREP (CCP4 v.6.4.0) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.025 | 1.680 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Rmerge | 0.745 | |
| Number of reflections | 62042 | |
| <I/σ(I)> | 13.52 | 1.8 |
| Completeness [%] | 99.2 | 97.05 |
| Redundancy | 6.9 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 292 | PEG 3350, Tris-Cl, MgCl2 |
