5F7S
Cycloalternan-degrading enzyme from Trueperella pyogenes
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 | CCD |
| Collection date | 2015-10-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 197.126, 104.663, 89.030 |
| Unit cell angles | 90.00, 90.74, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.300 |
| R-factor | 0.1718 |
| Rwork | 0.170 |
| R-free | 0.21122 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4kmq |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.526 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.074 | 0.564 |
| Number of reflections | 80180 | |
| <I/σ(I)> | 15.2 | 2.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 300 | Protein solution: 12.0 mg/ml, 0.5 M NaCl, 0.01 M Tris-HCl pH 8.3 Crystallization condition: PACT (Qiagen) C11: 0.2 M Calcium chloride, 0.1 m Hepes pH 7, and 25% (w/v) PEG 600 |
