5HXW
L-amino acid deaminase from Proteus vulgaris
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BSRF BEAMLINE 3W1A |
| Synchrotron site | BSRF |
| Beamline | 3W1A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-07-05 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 100.314, 104.575, 105.419 |
| Unit cell angles | 64.52, 73.06, 61.17 |
Refinement procedure
| Resolution | 94.630 - 2.630 |
| R-factor | 0.22282 |
| Rwork | 0.221 |
| R-free | 0.25198 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5i39 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.249 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 94.630 | 2.720 |
| High resolution limit [Å] | 2.630 | 2.630 |
| Number of reflections | 97176 | |
| <I/σ(I)> | 31 | |
| Completeness [%] | 97.2 | |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 285 | 5% m/v PEG 20000, 200mM MES,1mM cetyltrimethylammonium bromide |
