5COQ
The effect of valine to alanine mutation on InhA enzyme crystallization pattern and substrate binding loop conformation and flexibility
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-08 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 126.095, 91.903, 102.846 |
| Unit cell angles | 90.00, 106.45, 90.00 |
Refinement procedure
| Resolution | 46.067 - 2.300 |
| R-factor | 0.1632 |
| Rwork | 0.161 |
| R-free | 0.21220 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.130 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 48995 |
| <I/σ(I)> | 21.9 |
| Completeness [%] | 98.5 |
| Redundancy | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | Potassium sodium tartrate, PEG 3350 |
