3E4D
Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-03-01 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 68.433, 68.949, 95.648 |
| Unit cell angles | 92.41, 99.79, 98.47 |
Refinement procedure
| Resolution | 25.000 - 2.010 |
| R-factor | 0.183 |
| Rwork | 0.181 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB code 1PV1 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.207 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MrBUMP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.400 | 2.090 |
| High resolution limit [Å] | 2.010 | 2.020 |
| Rmerge | 0.058 | 0.288 |
| Number of reflections | 106354 | |
| <I/σ(I)> | 23.2 | 4.3 |
| Completeness [%] | 95.0 | 80 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | PEG 3350, MgCl2, Bis-Tris buffer, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
