6A6T
Crystal structure of the modified fructosyl peptide oxidase from Aspergillus nidulans with R61G mutation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-12-09 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 72.349, 72.349, 160.114 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.732 - 1.901 |
| R-factor | 0.2315 |
| Rwork | 0.230 |
| R-free | 0.26350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6a6r |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.420 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.057 | 0.405 |
| Number of reflections | 38889 | 1893 |
| <I/σ(I)> | 14.1 | |
| Completeness [%] | 99.6 | |
| Redundancy | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10.4 | 293 | 1.75 M ammonium sulfate, 0.2 M lithium sulfate, and 0.08 M CAPS (N-cyclohexyl-3-aminopropanesulfonic acid) buffer (pH 10.4) |
