3V89
The crystal structure of transferrin binding protein A (TbpA) from Neisseria meningitidis serogroup B in complex with the C-lobe of human transferrin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-07-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.054, 107.592, 130.719 |
| Unit cell angles | 90.00, 94.48, 90.00 |
Refinement procedure
| Resolution | 29.959 - 3.100 |
| R-factor | 0.2273 |
| Rwork | 0.224 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.125 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.2_865)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.210 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Number of reflections | 28265 | |
| <I/σ(I)> | 20.8 | 3.9 |
| Completeness [%] | 96.3 | 76.9 |
| Redundancy | 3.7 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 21% PEG 1000, 100mM sodium acetate buffer (pH 4.8), 200mM NaCl, 0.1% LDAO and 3% heptane-1,2,3-triol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
