3IPW
Crystal structure of hydrolase TatD family protein from Entamoeba histolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-08-07 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 83.392, 83.392, 90.405 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.950 |
| R-factor | 0.193 |
| Rwork | 0.191 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3e2v clipped to contain only homologous sections |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.303 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.073 | 0.470 |
| Number of reflections | 23615 | |
| <I/σ(I)> | 21.8 | 2.45 |
| Completeness [%] | 98.8 | 93.2 |
| Redundancy | 6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | JCSG+ condition D1, 24% PEG 1500, 20% glycerol, 44.6 mg/mL protein, crystal tracking ID 202317d1, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
