3LPG
Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-15 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 167.814, 76.934, 125.810 |
Unit cell angles | 90.00, 124.75, 90.00 |
Refinement procedure
Resolution | 30.859 - 2.425 |
R-factor | 0.206 |
Rwork | 0.204 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3k4d |
RMSD bond length | 0.004 |
RMSD bond angle | 1.023 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.859 | 2.477 |
High resolution limit [Å] | 2.425 | 2.425 |
Rmerge | 0.137 | |
Number of reflections | 44902 | |
<I/σ(I)> | 26.6 | 4.5 |
Completeness [%] | 89.5 | 77 |
Redundancy | 3.9 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 289 | 15% PEG 3350, 0.2 M MgAcetate, 0.02% sodium azide, 5 mM 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea, pH 7.4, vapor diffusion, hanging drop, temperature 289K |