3TBH
Crystal structure of O-Acetyl Serine Sulfhydrylase in complex with octapeptide derived from Serine Acetyl Transferase of Leishmania donovani
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-29 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 115.217, 62.440, 43.538 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 115.220 - 1.680 |
| R-factor | 0.1864 |
| Rwork | 0.185 |
| R-free | 0.22020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3spx |
| RMSD bond length | 0.031 |
| RMSD bond angle | 2.478 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 115.220 |
| High resolution limit [Å] | 1.680 |
| Number of reflections | 36632 |
| Completeness [%] | 99.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | KSCN, PEG 3350, pH 6.5, vapor diffusion, hanging drop, temperature 289K |
