1QLT
STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-10-15 |
| Detector | MARRESEARCH |
| Spacegroup name | I 4 |
| Unit cell lengths | 129.660, 129.660, 132.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.200 |
| R-factor | 0.21 * |
| Rwork | 0.210 |
| R-free | 0.26400 |
| Structure solution method | OTHER |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.020 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.089 | 0.226 |
| Total number of observations | 285553 * | |
| Number of reflections | 55414 | |
| <I/σ(I)> | 6 | 2.8 |
| Completeness [%] | 93.1 | 78.8 |
| Redundancy | 2.1 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 20 * | Mattevi, A., (1997) Proteins: Struct.,Funct., Genet., 27, 601. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 7.5 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 25 (mM) | |
| 3 | 1 | drop | sodium acetate | 50 (mM) | |
| 4 | 1 | drop | 0.01 (%(w/v)) | ||
| 5 | 1 | drop | PEG4000 | 3 (%(w/v)) | |
| 6 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 7 | 1 | reservoir | 0.02 (%(w/v)) | ||
| 8 | 1 | reservoir | PEG4000 | 6 (%(w/v)) |
