1OGH
Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-11-18 |
Detector | MARRESEARCH |
Spacegroup name | P 21 3 |
Unit cell lengths | 111.060, 111.060, 111.060 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.650 - 1.880 |
R-factor | 0.148 |
Rwork | 0.147 |
R-free | 0.18400 |
Structure solution method | SIRAS |
RMSD bond length | 0.018 |
RMSD bond angle | 1.630 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 1.920 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.042 | 0.136 |
Total number of observations | 417089 * | |
Number of reflections | 37385 | |
<I/σ(I)> | 52 | 21 |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 11.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 20 * | 3MG/ML PROTEIN VAPOUR DIFFUSION WITH MOTHER LIQUOR: 5% PEG8000, 0.1 M TRIS-HCL, PH8.5, pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | pH8.5 |
3 | 1 | reservoir | PEG8000 | 5 (%) | |
4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |