5I0F
Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with covalent intermediate
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 | 2015-10-26 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 195.127, 103.128, 44.094 |
| Unit cell angles | 90.00, 92.14, 90.00 |
Refinement procedure
| Resolution | 28.590 - 1.850 |
| R-factor | 0.1604 |
| Rwork | 0.159 |
| R-free | 0.18950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5f7s |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.428 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.089 | 0.721 |
| Number of reflections | 74285 | |
| <I/σ(I)> | 17.3 | 1.95 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein solution: 8.0 mg/ml, 0.5 M NaCl, 0.01 M Tris-HCl pH 8.3 Crystallization condition: PACT (Qiagen) B11: 0.2 M Calcium chloride, 0.1 m MES pH 6, and 20% (w/v) PEG 6000 |
