3B3X
Crystal structure of class A beta-lactamase of Bacillus licheniformis BS3 with aminocitrate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-03-04 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.665, 104.710, 63.884 |
Unit cell angles | 90.00, 93.96, 90.00 |
Refinement procedure
Resolution | 36.470 - 2.500 |
R-factor | 0.223 |
Rwork | 0.220 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w7f |
RMSD bond length | 0.016 |
RMSD bond angle | 1.834 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 63.758 | 36.470 | 2.640 |
High resolution limit [Å] | 2.500 | 7.910 | 2.500 |
Rmerge | 0.083 | 0.042 | 0.371 |
Total number of observations | 1645 | 3926 | |
Number of reflections | 17440 | ||
<I/σ(I)> | 7.6 | 10.8 | 1.9 |
Completeness [%] | 82.3 | 81.2 | 75.5 |
Redundancy | 1.9 | 2.9 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | hanging drop | 7.2 | 293 | 5micro-l of a protein solution (at a concentration of 38mg/ml in 50mM NaCl, 10mM Tris buffer, pH 7.2), 4micro-l of 8% PEG 6000 in 100mM sodium aminocitrate buffer (pH 3.4) plus 1micro-l of 0.1M urea additive, equilibrated against 1ml of a 20% PEG 6000, hanging drop, temperature 293K |