4ELC
Crystal structure of the catalytic domain of botulinum neurotoxin BoNT/A C134 mutant with MTSEA modified Cys-165
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-30 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.93950 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 65.290, 65.290, 200.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.950 - 1.800 |
| R-factor | 0.172 |
| Rwork | 0.169 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4el4 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.007 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.950 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.092 | 0.575 |
| Number of reflections | 41382 | |
| <I/σ(I)> | 17.37 | 5.1 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 7.68 | 5.97 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
