6O63
Crystal Structure of Arabidopsis thaliana Spermidine Synthase isoform 1 (AtSPDS1)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-11-01 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 89.536, 76.338, 90.192 |
Unit cell angles | 90.00, 104.68, 90.00 |
Refinement procedure
Resolution | 43.460 - 1.800 |
R-factor | 0.16583 |
Rwork | 0.165 |
R-free | 0.22209 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.796 |
Data reduction software | XDS (version Jan 2018) |
Data scaling software | STARANISO |
Phasing software | PHASER (2.8.2) |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.600 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.055 | 0.547 |
Number of reflections | 95958 | 4794 |
<I/σ(I)> | 14.1 | 2.5 |
Completeness [%] | 95.4 | 78.5 |
Redundancy | 4.1 | 4 |
CC(1/2) | 0.999 | 0.787 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 292 | 0.2 M ammonium sulfate, 0.1 M BIS-TRIS, 25% PEG 3350, cryoprotection 25% glycerol |