2VOV
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 72.990, 88.570, 101.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.300 - 1.350 |
R-factor | 0.194 |
Rwork | 0.193 |
R-free | 0.21100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vox |
RMSD bond length | 0.007 |
RMSD bond angle | 1.141 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.3.0021) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.300 | 1.420 |
High resolution limit [Å] | 1.350 | 1.350 |
Rmerge | 0.040 | 0.050 |
Number of reflections | 71009 | |
<I/σ(I)> | 8.6 | 1.6 |
Completeness [%] | 98.5 | 97.3 |
Redundancy | 5.2 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 36-45% AMMONIUM SULFATE, 0.1 M HEPES PH 7.25-7.75 |