1EXT
EXTRACELLULAR DOMAIN OF THE 55KDA TUMOR NECROSIS FACTOR RECEPTOR. CRYSTALLIZED AT PH3.7 IN P 21 21 21.
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 123 |
Detector technology | IMAGE PLATE |
Collection date | 1994-03-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.810, 83.060, 67.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.850 |
R-factor | 0.205 * |
Rwork | 0.203 |
R-free | 0.24300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ncf |
RMSD bond length | 0.009 |
RMSD bond angle | 25.290 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 11.000 * | 1.930 |
High resolution limit [Å] | 1.850 * | 1.850 |
Rmerge | 0.051 | |
Number of reflections | 37300 * | |
Completeness [%] | 97.0 | 77 |
Redundancy | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 3.7 | 293 * | Rodseth, L.E., (1994) J.Mol.Biol., 239, 332. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.5 (mg/ml) | |
2 | 1 | drop | PBS | 0.025ml | |
3 | 1 | drop | sodium formate | 50 (mM) | |
4 | 1 | drop | 1 (M) | ||
5 | 1 | reservoir | 1.7 (M) | ||
6 | 1 | reservoir | sodium formate | 100 (mM) |