5FJT
N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: G291D F323 mutant in complex with N-acetyl phenylalanine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 120 |
| Detector technology | PIXEL |
| Collection date | 2015-05-07 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 216.204, 216.204, 258.691 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 151.680 - 2.110 |
| R-factor | 0.16121 |
| Rwork | 0.160 |
| R-free | 0.18098 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4a6g |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.997 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 88.000 | 2.140 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.070 | 0.430 |
| Number of reflections | 133075 | |
| <I/σ(I)> | 25.3 | 6.5 |
| Completeness [%] | 99.9 | 99 |
| Redundancy | 12.5 | 12.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 100 MM TRIS HCL PH 8.0; 15% (W/V) PEG 4K; 800 MM SODIUM FORMATE; PROTEIN AT 8 MG PER ML |
