1K07
Native FEZ-1 metallo-beta-lactamase from Legionella gormanii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-04-29 |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.860, 76.850, 78.890 |
Unit cell angles | 90.00, 102.08, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.650 |
Rwork | 0.174 |
R-free | 0.19830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jt1 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.620 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.740 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.021 * | 0.037 * |
Total number of observations | 217456 * | |
Number of reflections | 61458 * | |
<I/σ(I)> | 21.9 | |
Completeness [%] | 97.9 | 96.9 |
Redundancy | 3.5 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 * | 20 * | 20% PEG4000, 0.2M ammonium sulfate, 0.010MM ZnCl2, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10.5 (mg/ml) | |
2 | 1 | drop | sodium cacodylate | 15 (mM) | pH6.0 |
3 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
4 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
5 | 1 | reservoir | 20000 (mM) | ||
6 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.0 |