2CB1
Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-05-20 |
| Detector | RIGAKU CCD |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 55.986, 86.392, 156.138 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 78.090 - 2.000 |
| R-factor | 0.19 |
| Rwork | 0.187 |
| R-free | 0.23400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e5f |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.028 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | |
| High resolution limit [Å] | 2.000 | 1.900 |
| Rmerge | 0.050 | 0.230 |
| Number of reflections | 25853 | |
| <I/σ(I)> | 33.95 | 5.04 |
| Completeness [%] | 99.3 | 95 |
| Redundancy | 6.9 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
