3HNC
Crystal structure of human ribonucleotide reductase 1 bound to the effector TTP
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 | 2008-04-15 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.980, 114.104, 219.283 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.530 - 2.410 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.231 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.000 | 40.000 | 2.380 |
High resolution limit [Å] | 2.300 | 4.950 | 2.300 |
Rmerge | 0.091 | 0.037 | 0.566 |
Number of reflections | 75994 | ||
<I/σ(I)> | 13.144 | ||
Completeness [%] | 97.8 | 94.5 | 95.9 |
Redundancy | 3.4 | 3.7 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | 298 | 0.1 M Tris-HCl pH 7.9, 0.2 M LiSO4, 19% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K |