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) |