1QMF
PENICILLIN-BINDING PROTEIN 2X (PBP-2X) ACYL-ENZYME COMPLEX
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-10-15 |
Detector | MARRESEARCH |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 129.910, 129.910, 139.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.800 |
R-factor | 0.239 |
Rwork | 0.239 |
R-free | 0.27100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | APO ENZYME |
RMSD bond length | 0.013 |
RMSD bond angle | 24.800 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS (0.5) |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.092 | 0.508 |
Number of reflections | 29276 | |
Completeness [%] | 97.9 | 92.2 * |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 25 * | 0.1M SODIUM ACETATE PH 4.5, 1.0-1.3M AMMONIUM SULFATE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris | 10 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | reservoir | sodium acetate | 0.1 (M) | |
5 | 1 | reservoir | ammonium sulfate | 1.0-1.3 (M) |