2FRG
Structure of the immunoglobulin-like domain of human TLT-1
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-05-24 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 47.095, 79.981, 25.780 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.190 |
R-factor | 0.17711 |
Rwork | 0.176 |
R-free | 0.19062 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Hybrid model containing structurally conserved residues of TREM-1 (1SMO chain A) NKp44(1HKF) and D1 domain of polymeric immunoglobulin receptor (1XED chain E). |
RMSD bond length | 0.010 |
RMSD bond angle | 1.452 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.230 |
High resolution limit [Å] | 1.190 | 1.190 |
Number of reflections | 31487 | |
<I/σ(I)> | 25.9 | 3.2 |
Completeness [%] | 98.2 | 87 |
Redundancy | 6.4 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | Mother liquor contained 15-19% w/w PEG6000, 0.5M Na/K phosphate pH 5.6. Protein solution contained 10mg/ml TLT-1 in 20mM Tris pH 8. Protein and mother liquor were mixed in equal proportions at 15 C, and hanging drops were suspended over mother liquor., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | Mother liquor contained 15-19% w/w PEG6000, 0.5M Na/K phosphate pH 5.6. Protein solution contained 10mg/ml TLT-1 in 20mM Tris pH 8. Protein and mother liquor were mixed in equal proportions at 15 C, and hanging drops were suspended over mother liquor., VAPOR DIFFUSION, HANGING DROP, temperature 293K |