5XA2
Crystal Structure of O-acetylserine sulfhydrylase from Planctomyces Limnophila
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2016-05-17 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 54.996, 90.041, 128.360 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.620 - 2.034 |
R-factor | 0.1626 |
Rwork | 0.160 |
R-free | 0.20470 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ho1 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.902 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.620 | 2.070 |
High resolution limit [Å] | 2.034 | 2.030 |
Rmerge | 0.050 | 0.273 |
Number of reflections | 37925 | |
<I/σ(I)> | 30.1 | 3.5 |
Completeness [%] | 90.5 | |
Redundancy | 6.4 | 3.5 |
CC(1/2) | 1.000 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 20% PEG 8000 100mM Tris pH8.5 200mM MgCl2 |