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 |