1JRH
COMPLEX (ANTIBODY/ANTIGEN)
Experimental procedure
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 85.740, 90.800, 101.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.246 |
Rwork | 0.246 |
R-free | 0.31400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 1BBJ 1bbc AND 2HFL |
RMSD bond length | 0.011 |
RMSD bond angle | 1.850 |
Data reduction software | MARXDS |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.950 |
High resolution limit [Å] | 2.800 | 2.820 |
Rmerge | 0.059 * | 0.288 * |
Total number of observations | 74824 * | |
Number of reflections | 19997 | 2465 * |
Completeness [%] | 98.8 | 98.1 |
Redundancy | 3.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.5 | 10%(W/V) PEG ME 5000, 0.5M NACL, 50MM BIS/TRIS, PH 5.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 17 (mg/ml) | |
2 | 1 | drop | Tris | 21 (mM) | |
3 | 1 | drop | 93 (mM) | ||
4 | 1 | drop | EDTA | 0.4 (mM) | |
5 | 1 | drop | PEG ME5000 | 1.4 (%(w/v)) | |
6 | 1 | drop | Bis-Tris | 7 (mM) | |
7 | 1 | reservoir | PEG ME5000 | 10 (%(w/v)) | |
8 | 1 | reservoir | 0.5 (M) | ||
9 | 1 | reservoir | Bis-Tris | 50 (mM) |