5CZK
Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)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 | 2012-10-22 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 169.140, 76.098, 125.831 |
Unit cell angles | 90.00, 125.30, 90.00 |
Refinement procedure
Resolution | 42.000 - 2.390 |
R-factor | 0.2032 |
Rwork | 0.200 |
R-free | 0.25580 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.223 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.000 | 2.480 |
High resolution limit [Å] | 2.390 | 2.390 |
Number of reflections | 51255 | |
<I/σ(I)> | 12.28 | 2.3 |
Completeness [%] | 99.0 | 91.1 |
Redundancy | 5.1 | 5.1 |
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, 1 mM 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea |