2C2I
Structure and function of Rv0130, a conserved hypothetical protein from M.tuberculosis
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 58.697, 108.708, 50.376 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.800 |
R-factor | 0.185 |
Rwork | 0.183 |
R-free | 0.22600 |
Structure solution method | OTHER |
RMSD bond length | 0.022 |
RMSD bond angle | 1.383 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 54.400 |
High resolution limit [Å] | 1.700 |
Rmerge | 0.080 |
Number of reflections | 38906 |
<I/σ(I)> | 20.5 |
Completeness [%] | 98.8 |
Redundancy | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |