5A0S
Apo-structure of metalloprotease Zmp1 variant E143A from Clostridium difficile
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-09-09 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.500, 72.390, 118.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.857 - 2.560 |
| R-factor | 0.2025 |
| Rwork | 0.200 |
| R-free | 0.25970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5a0p |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.629 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (in) |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.900 | 2.710 |
| High resolution limit [Å] | 2.560 | 2.560 |
| Rmerge | 0.170 | 0.810 |
| Number of reflections | 12587 | |
| <I/σ(I)> | 9.74 | 2.42 |
| Completeness [%] | 98.5 | 91.8 |
| Redundancy | 6.3 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 293 | 2.1 M D/L-MALIC ACID, PH 7.0 AT 293 K |
