5AH1
Structure of EstA from Clostridium botulinum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Collection date | 2013-06-10 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.240, 64.710, 69.790 |
| Unit cell angles | 90.00, 106.93, 90.00 |
Refinement procedure
| Resolution | 34.954 - 1.200 |
| R-factor | 0.1296 |
| Rwork | 0.129 |
| R-free | 0.14930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ku0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.182 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.020 | 1.260 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.060 | 0.410 |
| Number of reflections | 121016 | |
| <I/σ(I)> | 13 | 2.8 |
| Completeness [%] | 88.6 | 50.5 |
| Redundancy | 4.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.1 M TRIS, PH 8.5 AND 2 M AMMONIUM SULFATE |
