2Z15
Crystal structure of human Tob1 protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-06 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.9789, 0.9794, 0.964 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.064, 121.162, 152.553 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.440 - 2.300 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.24600 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.420 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 30540 | |
<I/σ(I)> | 21.6 | 4.94 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.76 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293 | 0.1M Sodium acetate trihydrate, 8% PEG4000, pH4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |