6WEP
Crystal structure of TS-DHFR from Cryptosporidium hominis with Apo-TS site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-18 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979180 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.822, 118.114, 153.048 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.270 - 2.790 |
R-factor | 0.2416 |
Rwork | 0.239 |
R-free | 0.28520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q0e |
RMSD bond length | 0.002 |
RMSD bond angle | 0.517 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.960 |
High resolution limit [Å] | 2.790 | 2.790 |
Number of reflections | 35381 | 5490 |
<I/σ(I)> | 14.12 | 1.61 |
Completeness [%] | 99.5 | 97 |
Redundancy | 12.6 | 11.8 |
CC(1/2) | 0.996 | 0.543 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295.15 | Well solution 18% PEG 8000, 0.2 M calcium acetate, 0.1 M sodium cacodylate Drop ratio 1:1 enzyme mix/well solution |