5K9A
Sortase A from Corynebacterium diphtheriae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 77.716, 77.716, 202.282 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.900 - 2.100 |
| R-factor | 0.1622 |
| Rwork | 0.161 |
| R-free | 0.19560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xwg |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.755 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.900 | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 5.700 | 2.100 |
| Rmerge | 0.142 | 0.046 | 0.916 |
| Number of reflections | 21872 | ||
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 99.7 | 97.4 | 100 |
| Redundancy | 15.4 | 13.2 | 15.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 1.6 M ammonium sulfate, 0.1 M MES/NaOH buffer, 10% 1,4-dioxane |
