2QZP
Crystal structure of mutation of an acylptide hydrolase/esterase from Aeropyrum pernix K1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-11-05 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.117, 102.183, 163.594 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.110 - 2.700 |
| R-factor | 0.226 |
| Rwork | 0.226 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ve6 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.177 | 0.777 |
| Number of reflections | 35191 | |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 5.8 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 291 | NaAc, PEG3000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
