6FRV
Structure of the catalytic domain of Aspergillus niger Glucoamylase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-18 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.933 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.369, 73.125, 102.880 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 59.670 - 2.300 |
R-factor | 0.2555 |
Rwork | 0.251 |
R-free | 0.34330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1agm |
RMSD bond length | 0.009 |
RMSD bond angle | 1.267 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmeas | 0.190 | 1.516 |
Number of reflections | 19454 | 1870 |
<I/σ(I)> | 6.3 | |
Completeness [%] | 99.5 | |
Redundancy | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 292 | PEG 3350, Hepes |