3LPF
Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-25 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 168.058, 77.409, 126.152 |
Unit cell angles | 90.00, 124.66, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.260 |
R-factor | 0.211 |
Rwork | 0.209 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3k4d |
RMSD bond length | 0.011 |
RMSD bond angle | 1.594 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
High resolution limit [Å] | 2.260 | 6.240 | 2.300 |
Rmerge | 0.128 | 0.095 | 0.465 |
Number of reflections | 59357 | ||
<I/σ(I)> | 13.7 | ||
Completeness [%] | 96.9 | 99.5 | 78.9 |
Redundancy | 6.8 | 7.3 | 5 |
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, 1mM 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea, pH 7.4, vapor diffusion, hanging drop, temperature 289K |