1BT5
CRYSTAL STRUCTURE OF THE IMIPENEM INHIBITED TEM-1 BETA-LACTAMASE FROM ESCHERICHIA COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.420, 62.010, 89.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.000 - 1.800 |
R-factor | 0.173 * |
Rwork | 0.173 |
R-free | 0.23800 |
Structure solution method | OTHER |
RMSD bond length | 0.010 |
RMSD bond angle | 23.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 1.890 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.059 * | 0.116 * |
Total number of observations | 84646 * | |
Number of reflections | 21770 | |
<I/σ(I)> | 20.9 | 8.7 |
Completeness [%] | 98.3 | 96.8 |
Redundancy | 3.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 7.8 | Jelsch, C., (1992) J. Mol. Biol., 223, 377. * |