3TRS
The crystal structure of aspergilloglutamic peptidase from Aspergillus niger
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.692, 65.842, 77.391 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.660 - 1.600 |
R-factor | 0.21 |
Rwork | 0.208 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y43 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.925 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.640 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.071 | 0.309 |
Number of reflections | 37983 | |
<I/σ(I)> | 12.25 | 3.24 |
Completeness [%] | 95.9 | 85.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 2.7 | 277 | 1.3M AMMONIUM SULFATE, 0.1M GLYCINE BUFFER (PH 2.7), 5% (V/V) DMSO, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K |