2XL9
Structure and metal-loading of a soluble periplasm cupro-protein: Zn- CucA-closed (SeMet)
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 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.750, 96.970, 114.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.110 - 2.060 |
| R-factor | 0.19224 |
| Rwork | 0.190 |
| R-free | 0.23689 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.298 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.000 | 2.170 |
| High resolution limit [Å] | 2.060 | 2.060 |
| Rmerge | 0.097 | 0.320 |
| Number of reflections | 31723 | |
| <I/σ(I)> | 9.6 | 2.5 |
| Completeness [%] | 96.3 | 80.3 |
| Redundancy | 3.4 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.8 | 0.1M TRIS PH8.8, 22% PEG 8000, 0.5MM ZNSO4 |
