3HSU
Functional roles of the 6-s-cysteinyl, 8 alpha-N1-histidyl FAD in Glucooligosaccharide Oxidase from Acremonium strictum
Replaces: 3E0TExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-24 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.483, 97.570, 98.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.880 - 1.690 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zr6 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.310 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.750 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.061 | 0.700 |
| Number of reflections | 62403 | |
| <I/σ(I)> | 42.7 | 2.2 |
| Completeness [%] | 98.0 | 87 |
| Redundancy | 13.5 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 25% PEG MME 550, 10mM ZnSO4, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
