2Q3C
2.1 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) Holoenzyme From MYCOBACTERIUM TUBERCULOSIS in Complex with the Inhibitory Peptide DFSI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2007-03-03 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 72.458, 72.458, 178.936 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.230 - 2.100 |
| R-factor | 0.18826 |
| Rwork | 0.187 |
| R-free | 0.20747 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2q3b Holoenzyme |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.195 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.660 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.089 | 0.352 |
| Number of reflections | 26571 | |
| <I/σ(I)> | 11.5 | 3.3 |
| Completeness [%] | 93.2 | 96.2 |
| Redundancy | 5.1 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1 M HEPES, 80% MPD, 4 mM DFSI-peptide, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
