4EUG
Crystallographic and Enzymatic Studies of an Active Site Variant H187Q of Escherichia Coli Uracil DNA Glycosylase: Crystal Structures of Mutant H187Q and its Uracil Complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-07-15 |
Detector | BRUKER |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.100, 59.000, 63.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 99.000 - 1.400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eug |
RMSD bond length | 0.010 |
RMSD bond angle | 0.028 |
Data reduction software | X-GEN |
Data scaling software | X-GEN |
Phasing software | SHELXS |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 1.490 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.105 | 0.320 |
Number of reflections | 77493 | |
<I/σ(I)> | 18.7 | 4.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.4 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 20 * | Xiao, G., (1999) Proteins Struct.Funct.Genet., 35, 13. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14.9 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 0.2 (M) | |
3 | 1 | reservoir | PEG4000 | 30 (%) | |
4 | 1 | reservoir | Tris | 0.1 (M) |