5UBJ
Structure of an alpha-L-arabinofuranosidase (GH62) from Aspergillus nidulans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE W01B-MX2 |
| Synchrotron site | LNLS |
| Beamline | W01B-MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-02-25 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.4586 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.562, 57.529, 49.371 |
| Unit cell angles | 90.00, 104.98, 90.00 |
Refinement procedure
| Resolution | 28.764 - 1.700 |
| R-factor | 0.1458 |
| Rwork | 0.144 |
| R-free | 0.17770 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4o8n |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.945 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.21) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.120 | 41.120 | 1.730 |
| High resolution limit [Å] | 1.700 | 9.000 | 1.700 |
| Rmerge | 0.054 | 0.036 | 0.635 |
| Rmeas | 0.065 | 0.045 | 0.834 |
| Rpim | 0.036 | 0.026 | 0.534 |
| Total number of observations | 72250 | 513 | 2502 |
| Number of reflections | 24535 | ||
| <I/σ(I)> | 14.7 | 39.7 | 1.8 |
| Completeness [%] | 96.8 | 94.4 | 88.9 |
| Redundancy | 2.9 | 2.9 | 2.1 |
| CC(1/2) | 0.997 | 0.977 | 0.682 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 32 % 2-Methyl-2,4-pentanediol, 10 % PEG8000, 0.1M calcium chloride, 0.1 M sodium acetate |
