2ZUK
The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae complexed with epsilon caprolactam (different binding mode)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-29 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.581, 60.653, 105.315 |
| Unit cell angles | 90.00, 103.07, 90.00 |
Refinement procedure
| Resolution | 40.290 - 2.410 |
| R-factor | 0.19427 |
| Rwork | 0.191 |
| R-free | 0.25141 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sft |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.359 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.088 | 0.359 |
| Number of reflections | 26897 | |
| Completeness [%] | 98.8 | 98.6 |
| Redundancy | 4.8 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.7 | 293 | 30% PEG4000, 0.2M magnesium chloride, 0.1M Tris/HCl (pH8.7), 2.9% Sucrose, 42microM PLP, 20mM epsilon-caprolactam, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
