1RJ8
The crystal structure of TNF family member EDA-A2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-01-24 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.723, 161.337, 51.023 |
Unit cell angles | 90.00, 105.24, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.230 |
R-factor | 0.2043 |
Rwork | 0.200 |
R-free | 0.24100 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | EDA-A1 trimer containing residues 248-307 319-333 347-390 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.160 * |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.07) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.330 |
High resolution limit [Å] | 2.230 | 2.230 |
Rmerge | 0.030 | 0.079 * |
Total number of observations | 101523 * | |
Number of reflections | 37259 | |
<I/σ(I)> | 23 | 9.5 |
Completeness [%] | 96.8 | 93.1 * |
Redundancy | 2.7 | 2.51 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 292 | 0.2M NaCl, 0.1M Hepes, 25% Peg 3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 19K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | reservoir | PEG3350 | 25 (%) | |
3 | 1 | reservoir | 0.2 (M) | ||
4 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |