2IID
Structure of L-amino acid oxidase from Calloselasma rhodostoma in complex with L-phenylalanine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Wavelength(s) | 0.652549 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 78.760, 154.003, 103.183 |
Unit cell angles | 90.00, 109.52, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.800 |
R-factor | 0.17354 |
Rwork | 0.172 |
R-free | 0.21006 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1f8r |
RMSD bond length | 0.013 |
RMSD bond angle | 1.489 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.101 | 0.418 |
Number of reflections | 211556 | |
<I/σ(I)> | 11.9 | 3.1 |
Completeness [%] | 99.5 | 100 |
Redundancy | 4.06 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 290 | 20-22% PEG 4000, 200mM Li2SO4, 10% glycerol, 100mM Tris-HCl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 290K |