4FK9
High Resolution Structure of the Catalytic Domain of Mannanase SActE_2347 from Streptomyces sp. SirexAA-E
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2012-04-18 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 62.805, 102.360, 45.346 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.765 - 1.060 |
| R-factor | 0.1187 |
| Rwork | 0.118 |
| R-free | 0.13150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.232 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8_1061) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.080 |
| High resolution limit [Å] | 1.060 | 2.880 | 1.060 |
| Rmerge | 0.063 | 0.048 | 0.315 |
| Number of reflections | 130004 | ||
| <I/σ(I)> | 12.8 | ||
| Completeness [%] | 97.7 | 90.3 | 95.3 |
| Redundancy | 3.5 | 3.6 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |






