1ELK
VHS domain of TOM1 protein from H. sapiens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-11-22 |
Detector | ADSC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.070, 52.860, 73.220 |
Unit cell angles | 90.00, 99.75, 90.00 |
Refinement procedure
Resolution | 15.670 - 1.500 |
R-factor | 0.193 * |
Rwork | 0.193 |
R-free | 0.22100 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.9) |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.076 * | 0.276 |
Number of reflections | 49338 | 4775 * |
<I/σ(I)> | 22.4 | |
Completeness [%] | 97.0 | 94.8 |
Redundancy | 3.36 | 2.71 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 20 * | 20%PEG8000, 100 mM HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 50 (mM) | ||
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | EDTA | 0.1 (mM) | |
4 | 1 | drop | dithiothreitol | 10 (mM) | |
5 | 1 | drop | protain | 12-18 (mg/ml) | |
6 | 1 | reservoir | PEG8000 | 20 (%) | |
7 | 1 | reservoir | HEPES | 100 (mM) |