3AUL
Crystal structure of wild-type Lys48-linked diubiquitin in an open conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-07 |
Detector | Bruker DIP-6040 |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 23.820, 56.690, 46.610 |
Unit cell angles | 90.00, 93.33, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.390 |
R-factor | 0.20525 |
Rwork | 0.203 |
R-free | 0.25166 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tbe |
RMSD bond length | 0.012 |
RMSD bond angle | 1.192 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.510 |
High resolution limit [Å] | 2.380 | 2.380 |
Rmerge | 0.149 | 0.276 |
Number of reflections | 4854 | |
<I/σ(I)> | 6.2 | 4.3 |
Completeness [%] | 96.5 | 84.2 |
Redundancy | 3.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 20% PEG 3350, 0.2M litium sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |