1QKZ
Fab fragment (MN14C11.6) in complex with a peptide antigen derived from Neisseria meningitidis P1.7 serosubtype antigen and domain II from Streptococcal protein G
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.5 |
| Synchrotron site | SRS |
| Beamline | PX9.5 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.482, 63.099, 89.374 |
| Unit cell angles | 90.00, 81.54, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.950 |
| R-factor | 0.209 |
| Rwork | 0.205 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1igc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.029 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.040 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.037 * | 0.125 * |
| Total number of observations | 180259 * | |
| Number of reflections | 34633 | |
| <I/σ(I)> | 17.2 | |
| Completeness [%] | 98.9 | 96 |
| Redundancy | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5 | 293 * | pH 5.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Fab | 11 (mg/ml) | |
| 2 | 1 | drop | protein G | 8.1 (mg/ml) | |
| 3 | 1 | drop | peptide | 2.2 (mg/ml) | |
| 4 | 1 | reservoir | sodium acetate | 50 (mM) | |
| 5 | 1 | reservoir | PEG6000 | 24 (%(w/v)) |
