2Q3D
2.2 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) From MYCOBACTERIUM TUBERCULOSIS in Complex with the Reaction Intermediate ALPHA-AMINOACRYLATE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2006-10-19 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 71.785, 71.785, 181.179 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.350 - 2.200 |
| R-factor | 0.19641 |
| Rwork | 0.194 |
| R-free | 0.24943 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2q3b Holoenzyme |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.419 |
| 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] | 71.800 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.091 | 0.499 |
| Number of reflections | 24607 | |
| <I/σ(I)> | 14.2 | 2.4 |
| Completeness [%] | 98.9 | 99.8 |
| Redundancy | 5.4 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.2 | 293 | 0.1 M HEPES, 80% MPD. SOAKED WITH 1 mM O-ACETYL-SERINE FOR 30 MINUTES BEFORE FREEZING., pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
