1D2S
CRYSTAL STRUCTURE OF THE N-TERMINAL LAMININ G-LIKE DOMAIN OF SHBG IN COMPLEX WITH DIHYDROTESTOSTERONE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 1999-04-01 |
Detector | MARRESEARCH |
Spacegroup name | H 3 2 |
Unit cell lengths | 104.040, 104.040, 84.430 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 1.550 |
R-factor | 0.21 |
Rwork | 0.205 |
R-free | 0.25100 |
RMSD bond length | 0.013 |
RMSD bond angle | 0.030 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MLPHARE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.750 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.042 | 0.234 |
Number of reflections | 24678 | |
<I/σ(I)> | 16.5 | |
Completeness [%] | 96.4 | 95 |
Redundancy | 3.4 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 13 (mg/ml) | |
2 | 1 | drop | HEPES | 50 (mM) | |
3 | 1 | drop | 2.5 (mM) | ||
4 | 1 | drop | 5alpha-DHT | 0.003 (mM) | |
5 | 1 | reservoir | isopropanol | 20 (%) | |
6 | 1 | reservoir | PEG400 | 10 (%) | |
7 | 1 | reservoir | HEPES | 100 (mM) |