2XD1
ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS
Replaces: 2UWYReplaces: 2BG4Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 96.600, 102.300, 146.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.220 - 3.000 |
R-factor | 0.17 |
Rwork | 0.161 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bg1 |
RMSD bond length | 0.034 |
RMSD bond angle | 3.032 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.200 | 3.100 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.070 | 0.250 |
Number of reflections | 26716 | |
<I/σ(I)> | 8.9 | 2.7 |
Completeness [%] | 100.0 | 99 |
Redundancy | 4 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 50 MM HEPES, 0.8 M AMMONIUM SULFATE, 3.2 M SODIUM CHLORIDE, PH 7.00 |