1G1T
CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH SLEX
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01-01 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.506, 72.387, 77.576 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.500 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.420 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.041 | 0.220 |
Total number of observations | 260283 * | |
Number of reflections | 29493 | |
<I/σ(I)> | 47.6 | |
Completeness [%] | 92.4 | 62 |
Redundancy | 8.8 | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 18 * | HEPES, Tris-HCl, CaCl2, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | drop | HEPES | 100 (mM) | |
3 | 1 | drop | Tris-HCl | 10 (mM) | |
4 | 1 | drop | 200 (mM) | ||
5 | 1 | drop | PEG4000 | 15 (%(w/v)) |