2C1I
Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-11-11 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.275, 79.239, 100.377 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.350 |
| R-factor | 0.189 |
| Rwork | 0.188 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c1g |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.569 |
| Data reduction software | HKL |
| Data scaling software | HKL |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.400 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.070 | 0.440 |
| Number of reflections | 93309 | |
| <I/σ(I)> | 16.8 | 2.8 |
| Completeness [%] | 94.3 | 94.5 |
| Redundancy | 5.4 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | PROTEIN WAS CRYSTALLIZED FROM 35% PEG 200, 5% PEG 3000, 100 MM MES, PH 6; THEN SOAKED IN 10 MM ZNCL2. FOLLOWED BY SOAK IN 20%PEG 200, 100MM MES, PH 6 |
