3KVE
Structure of native L-amino acid oxidase from Vipera ammodytes ammodytes: stabilization of the quaternary structure by divalent ions and structural changes in the dynamic active site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X13 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-10 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.8 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 196.978, 95.839, 108.442 |
Unit cell angles | 90.00, 92.53, 90.00 |
Refinement procedure
Resolution | 27.400 - 2.570 |
R-factor | 0.19537 |
Rwork | 0.191 |
R-free | 0.27609 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f8r |
RMSD bond length | 0.012 |
RMSD bond angle | 1.523 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.400 | 2.660 |
High resolution limit [Å] | 2.570 | 2.570 |
Rmerge | 0.172 | 0.448 |
Number of reflections | 62717 | |
<I/σ(I)> | 10.6 | |
Completeness [%] | 97.1 | 74.7 |
Redundancy | 7.1 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |