3QVW
L-myo-inositol 1-phosphate synthase from Archaeoglobus fulgidus mutant K278A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-02-15 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 82.260, 89.940, 104.865 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 68.200 - 2.000 |
R-factor | 0.21836 |
Rwork | 0.215 |
R-free | 0.28198 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u1i |
RMSD bond length | 0.018 |
RMSD bond angle | 1.927 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 68.200 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.088 | 0.384 |
Number of reflections | 26097 | |
<I/σ(I)> | 7.7 | 2.1 |
Completeness [%] | 97.9 | 96.8 |
Redundancy | 2.6 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2 M calcium chloride, 14% PEG400, 15% PEG1500, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |