3KVD
Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-02-22 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.2 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 83.097, 83.097, 71.301 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 60.000 - 2.000 |
| R-factor | 0.22844 |
| Rwork | 0.227 |
| R-free | 0.24988 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w80 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.541 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 2.200 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.220 | 0.470 |
| Number of reflections | 17912 | |
| <I/σ(I)> | 6.6 | 1.8 |
| Completeness [%] | 98.0 | 90.7 |
| Redundancy | 3.9 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | 25% PEG 2000 MME, 300 mM Na acetate, 100 mM Tris, pH 7.5, VAPOR DIFFUSION, temperature 293K |
