4M6J
Crystal structure of human dihydrofolate reductase (DHFR) bound to NADPH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-05 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9795 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 38.958, 65.525, 152.251 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.486 - 1.201 |
R-factor | 0.1639 |
Rwork | 0.163 |
R-free | 0.18450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dls |
RMSD bond length | 0.009 |
RMSD bond angle | 1.480 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.230 |
High resolution limit [Å] | 1.200 | 1.200 |
Number of reflections | 59318 | |
<I/σ(I)> | 14 | 2 |
Completeness [%] | 96.8 | 76.9 |
Redundancy | 6.5 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 277 | 24% PEG6000, 100 mM Tris, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |