3AB0
Crystal structure of complex of the Bacillus anthracis major spore surface protein BclA with ScFv antibody fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 125.448, 125.448, 125.448 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.350 - 3.090 |
| R-factor | 0.20029 |
| Rwork | 0.197 |
| R-free | 0.26471 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2z5w 1qok |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.970 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0101) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.350 | 3.200 |
| High resolution limit [Å] | 3.090 | 3.090 |
| Rmerge | 0.170 | 0.920 |
| Number of reflections | 11525 | |
| <I/σ(I)> | 18.8 | 1 |
| Completeness [%] | 98.2 | 80 |
| Redundancy | 18.1 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 20% PEG 3350, 0.2M potassium acetate, 25% PEG 3350, 0.2M magnesium chloride, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
