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 |