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 |