1DY6
Structure of the imipenem-hydrolyzing beta-lactamase SME-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 291 |
Detector technology | DIFFRACTOMETER |
Detector | ENRAF-NONIUS FAST |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.500, 51.720, 71.690 |
Unit cell angles | 90.00, 118.62, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.130 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MODIFIED NMC-A BETA-LACTAMASE (1BUE) SOFTWARE USED: AMORE |
RMSD bond length | 0.007 |
RMSD bond angle | 1.440 |
Data reduction software | MADNESS |
Data scaling software | Agrovata |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.130 | 2.130 * |
Rmerge | 0.049 * | 0.216 * |
Total number of observations | 55772 * | |
Number of reflections | 24447 | 1601 * |
Completeness [%] | 82.0 | 30.1 * |
Redundancy | 2.3 | 2.1 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 17% PEG 4000, 0.2 M AMMONIUM ACETATE, 0.1 M TRIS-HCL, PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 17 (%) | |
2 | 1 | reservoir | ammonium acetate | 0.2 (M) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) |