1ODE
Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL45XU |
Synchrotron site | SPring-8 |
Beamline | BL45XU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-10-15 |
Detector | RIGAKU IMAGE PLATE RAXIS V |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.319, 78.540, 86.035 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.020 - 1.650 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dbf |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.064 | 0.383 |
Number of reflections | 174516 | |
<I/σ(I)> | 23.5 | 2.4 |
Completeness [%] | 99.5 | 99.5 |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 8.4 | PROTEIN WAS CRYSTALLIZED USING MICRO BATCH METHOD UNDER OIL FROM 27.5% PEG 4000, 10% DIOXANE AND 100 MM, TRIS/HCL(PH 8.4). |