5I0G
Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with cycloalternan
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) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 196.368, 103.900, 44.798 |
| Unit cell angles | 90.00, 90.32, 90.00 |
Refinement procedure
| Resolution | 28.480 - 2.150 |
| R-factor | 0.1737 |
| Rwork | 0.172 |
| R-free | 0.21046 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5f7s |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.377 |
| 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 | 2.190 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.094 | 0.528 |
| Number of reflections | 48835 | |
| <I/σ(I)> | 10.9 | 1.9 |
| Completeness [%] | 99.4 | 97.5 |
| Redundancy | 3.8 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Protein solution: 5.3 mg/ml, 0.25 M NaCl, 0.01 M Tris-HCl pH 8.3 Crystallization condition: JCSG+ (Qiagen) G7: 0.1 M Succinic acid (pH 7.0) and 15% (w/v) PEG 3350 |
