3IQH
Structure of O-Acetylserine Sulfhydrylase in Complex with Peptide MNYDI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 130 |
Detector technology | IMAGE PLATE |
Collection date | 2009-01-12 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | I 41 |
Unit cell lengths | 112.153, 112.153, 45.728 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.440 - 1.900 |
R-factor | 0.16503 |
Rwork | 0.163 |
R-free | 0.20869 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y7l |
RMSD bond length | 0.014 |
RMSD bond angle | 1.390 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.440 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.056 | 0.230 |
Number of reflections | 20150 | |
<I/σ(I)> | 21.6 | 6.3 |
Completeness [%] | 89.0 | 69.5 |
Redundancy | 4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | HEPES, Ammonium Sulfate, PEG 400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |