4KG6
Crystal Structure of AmpC beta-lactamase N152G Mutant from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-06-28 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 163.773, 79.660, 129.288 |
Unit cell angles | 90.00, 104.01, 90.00 |
Refinement procedure
Resolution | 27.500 - 1.750 |
R-factor | 0.16147 |
Rwork | 0.159 |
R-free | 0.20030 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.021 |
RMSD bond angle | 2.076 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Number of reflections | 162537 | |
Completeness [%] | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.7 | 296 | 1.7M potassium phosphate, 3.5mg/ml AmpC, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 296K |