2NM1
Structure of BoNT/B in complex with its protein receptor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-09 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.820, 97.520, 113.570 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.810 - 2.150 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z0h |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.076 | 0.507 |
| Number of reflections | 32377 | |
| <I/σ(I)> | 12.9 | 3 |
| Completeness [%] | 99.5 | 96.1 |
| Redundancy | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 293 | 13% PEG 6000, 0.1M Hepes, pH 7.0, EVAPORATION, temperature 293K |
