1E7S
GDP 4-keto-6-deoxy-D-mannose epimerase reductase K140R
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 103.400, 103.400, 75.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 12.000 - 1.500 |
Rwork | 0.126 |
R-free | 0.16200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bws |
RMSD bond length | 0.014 |
RMSD bond angle | 0.029 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.067 | |
Number of reflections | 73654 | |
<I/σ(I)> | 8.65 | 2.1 |
Completeness [%] | 98.8 | 97.7 |
Redundancy | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.5 | 21 * | 1.5 M LITHIUM SULPHATE, PH 6.5 0.1M TRIS BUFFER 21C |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 11-20 (mg/ml) | |
2 | 1 | 2 | lithium sulfate | 1.5 (M) | |
3 | 1 | 2 | MES | 0.1 (M) | orTris |