6PFE
Crystal structure of TS-DHFR from Cryptosporidium hominis in complex with NADPH, FdUMP and 2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)-4-methoxybenzoic acid.
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 | 2018-11-15 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.979200 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 212.859, 115.641, 219.899 |
Unit cell angles | 90.00, 95.00, 90.00 |
Refinement procedure
Resolution | 49.438 - 2.812 |
R-factor | 0.2274 |
Rwork | 0.227 |
R-free | 0.25720 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q0e |
RMSD bond length | 0.002 |
RMSD bond angle | 0.552 |
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 | 2.970 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 124669 | 17614 |
<I/σ(I)> | 5.78 | 0.83 |
Completeness [%] | 95.5 | 84.1 |
Redundancy | 6 | 5.3 |
CC(1/2) | 0.984 | 0.500 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295.15 | Well Solution 18 % PEG 6000, 0.2 M ammonium sulfate, 0.06 M lithium sulfate, 0.1 M Tris Drop Ratio 2:1 enzyme mix/well solution |