5I39
High resolution structure of L-amino acid deaminase from Proteus vulgaris with the deletion of the specific insertion sequence
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 | 2007-07-05 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.979 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.265, 63.708, 125.028 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.200 |
R-factor | 0.14161 |
Rwork | 0.141 |
R-free | 0.15683 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.370 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.072 | |
Number of reflections | 139986 | |
<I/σ(I)> | 34.1 | |
Completeness [%] | 97.8 | |
Redundancy | 10.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 285 | 10% PEG 8,000, 0.1 M Hepes pH 7.5, 10% Ethylene Glycol |