8H1W
Serine Palmitoyltransferase from Sphingobacterium multivorum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-12-11 |
Detector | RAYONIX MX225-HS |
Wavelength(s) | 0.9 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 61.612, 61.612, 208.349 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.604 - 1.400 |
Rwork | 0.169 |
R-free | 0.20170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3a2b |
RMSD bond length | 0.013 |
RMSD bond angle | 1.895 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.480 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 80227 | 12715 |
<I/σ(I)> | 20.6 | |
Completeness [%] | 100.0 | |
Redundancy | 10.8 | |
CC(1/2) | 1.000 | 0.848 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 297 | PEG4000, sodium acetate, Tris-HCl |