6PFF
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-cyanobenzoic 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 | 2016-08-16 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979180 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 213.424, 116.794, 221.760 |
Unit cell angles | 90.00, 95.69, 90.00 |
Refinement procedure
Resolution | 48.817 - 2.982 |
R-factor | 0.21 |
Rwork | 0.208 |
R-free | 0.23930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q0e |
RMSD bond length | 0.002 |
RMSD bond angle | 0.534 |
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 | 3.160 |
High resolution limit [Å] | 2.980 | 2.980 |
Number of reflections | 108730 | 15852 |
<I/σ(I)> | 9.62 | 1.9 |
Completeness [%] | 98.2 | 89.3 |
Redundancy | 3.7 | 3.6 |
CC(1/2) | 0.993 | 0.829 |
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 |