1W28
Conformational flexibility of the C-terminus with implications for substrate binding and catalysis in a new crystal form of deacetoxycephalosporin C synthase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 138.000, 138.000, 48.400 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.180 - 2.300 |
| R-factor | 0.198 |
| Rwork | 0.197 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dcs |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.288 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.040 | 0.310 |
| Number of reflections | 23763 | |
| <I/σ(I)> | 32 | 3.6 |
| Completeness [%] | 99.4 | 98.4 |
| Redundancy | 4 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 100 MM HEPES-NAOH PH 8, 0.9-1.1 M AMSO4 |
