3BFC
class A beta-lactamase SED-G238C complexed with imipenem
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-11-16 |
Detector | MARRESEARCH |
Wavelength(s) | 0.984 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 188.436, 73.399, 105.050 |
Unit cell angles | 90.00, 122.36, 90.00 |
Refinement procedure
Resolution | 35.000 - 2.200 |
R-factor | 0.215 |
Rwork | 0.206 |
R-free | 0.24200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3bfd |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 60669 | |
<I/σ(I)> | 8.2 | 2.87 |
Completeness [%] | 98.4 | 90.4 |
Redundancy | 3.9 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 35% PEG MME 2000, 200mM KSCN, 100mM SODIUM CACODYLATE pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |