5OHX
Structure of active cystathionine B-synthase from Apis mellifera
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR-H |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-10-04 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.542 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 86.143, 96.099, 180.684 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.360 - 3.200 |
R-factor | 0.1986 |
Rwork | 0.197 |
R-free | 0.23130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3pc2 |
RMSD bond length | 0.003 |
RMSD bond angle | 1.128 |
Data reduction software | HKL-2000 |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.400 | 3.300 |
High resolution limit [Å] | 3.200 | 3.200 |
Number of reflections | 25365 | |
<I/σ(I)> | 10.2 | 2.6 |
Completeness [%] | 99.7 | |
Redundancy | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 10% PEG 6000, 100 mM HEPES pH 7.5, 5% MPD |