2ZM2
Structure of 6-aminohexanoate-dimer hydrolase, A61V/A124V/R187S/F264C/G291R/G338A/D370Y mutant (Hyb-S4M94)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-18 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 96.442, 96.442, 113.496 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.640 - 1.550 |
| R-factor | 0.179 |
| Rwork | 0.179 |
| R-free | 0.19200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wyb |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.900 |
| 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 | 1.610 |
| High resolution limit [Å] | 1.500 | 1.550 |
| Rmerge | 0.125 | 0.446 |
| Number of reflections | 96878 | |
| <I/σ(I)> | 44.91 | 4.26 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.9 | 10.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 283 | 2.2M ammonium sulfate, 0.2M lithium sulfate, 0.1M MES, pH 6.50, temperature 283K |
