3A9K
Crystal structure of the mouse TAB3-NZF in complex with Lys63-linked di-ubiquitin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-29 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 29.900, 71.018, 71.562 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.720 - 1.400 |
R-factor | 0.18875 |
Rwork | 0.187 |
R-free | 0.21789 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3a9j |
RMSD bond length | 0.011 |
RMSD bond angle | 1.409 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.050 | 0.347 |
Number of reflections | 30844 | |
<I/σ(I)> | 36.8 | 2.78 |
Completeness [%] | 97.8 | 93.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 100mM Bis-Tris-HCl (pH 6.5), 21% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |