6PFA
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)methyl)benzoic acid.
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 | 2016-10-16 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979180 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 213.210, 117.294, 222.817 |
Unit cell angles | 90.00, 95.72, 90.00 |
Refinement procedure
Resolution | 48.933 - 2.790 |
R-factor | 0.2222 |
Rwork | 0.221 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q0e |
RMSD bond length | 0.002 |
RMSD bond angle | 0.494 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((1.15.2_3472: 000)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.950 |
High resolution limit [Å] | 2.790 | 2.790 |
Number of reflections | 135631 | 21167 |
<I/σ(I)> | 10.3 | 1.26 |
Completeness [%] | 99.2 | 96.3 |
Redundancy | 3.7 | 3.6 |
CC(1/2) | 0.996 | 0.782 |
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 |