2XL7
Structure and metal-loading of a soluble periplasm cupro-protein: Cu- 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 QUANTUM 210 |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 88.483, 88.483, 192.419 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 44.240 - 2.400 |
R-factor | 0.17609 |
Rwork | 0.174 |
R-free | 0.21317 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2xl9 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.298 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.100 | 0.340 |
Number of reflections | 18072 | |
<I/σ(I)> | 13.6 | 4.9 |
Completeness [%] | 99.7 | 100 |
Redundancy | 6 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 0.1 M HEPES PH 7.5, 20% (W/V) PEG 8000, 0.5MM CUSO4 |