8DAZ
Crystal structure of DMATS1 prenyltransferase in complex with L-Trp and GSPP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-02-16 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.979 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 89.832, 107.357, 179.301 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 92.110 - 2.490 |
R-factor | 0.2371 |
Rwork | 0.236 |
R-free | 0.26080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Alphafold |
RMSD bond length | 0.005 |
RMSD bond angle | 0.910 |
Data scaling software | STARANISO |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 92.110 | 2.640 |
High resolution limit [Å] | 2.490 | 2.490 |
Rmerge | 0.109 | 1.420 |
Rpim | 0.031 | 0.396 |
Number of reflections | 51807 | 2592 |
<I/σ(I)> | 13.2 | 2.1 |
Completeness [%] | 94.8 | 74.7 |
Redundancy | 13.4 | |
CC(1/2) | 0.998 | 0.708 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.9 | 294 | 7.5 mg/mL protein, 0.1 M Tris-HCl (pH 8.8), 0.6 M NaCl, 24% (v/v) PEG 3,350 |