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 |
