3QW2
L-myo-inositol 1-phosphate synthase from Archaeoglobus mutant N255A
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 | 2005-03-11 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 91.512, 88.036, 103.727 |
Unit cell angles | 90.00, 94.91, 90.00 |
Refinement procedure
Resolution | 103.140 - 2.590 |
R-factor | 0.18896 |
Rwork | 0.185 |
R-free | 0.26735 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u1i |
RMSD bond length | 0.015 |
RMSD bond angle | 1.662 |
Data reduction software | CrystalClear |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 103.140 | 2.640 |
High resolution limit [Å] | 2.590 | 2.590 |
Rmerge | 0.174 | 0.830 |
Number of reflections | 46724 | |
<I/σ(I)> | 8.5 | 1.2 |
Completeness [%] | 96.4 | 96.2 |
Redundancy | 2.1 | 1.5 |
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 |