1HTN
HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-10 |
| Detector | RIGAKU |
| Spacegroup name | H 3 |
| Unit cell lengths | 89.140, 89.140, 75.770 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.800 |
| R-factor | 0.223 |
| Rwork | 0.223 |
| R-free | 0.29200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2msb |
| RMSD bond length | 0.012 |
| RMSD bond angle | 24.000 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.870 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.107 | 0.519 |
| Number of reflections | 5529 | |
| <I/σ(I)> | 6.7 | 1.5 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 5.5 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 293 * | THE PROTEIN WAS CRYSTALLIZED BY THE REVERSE SALTING IN METHOD FROM A DROP CONTAINING 12.5-25 MM TRIS-HCL, PH 8.0, 25-50 MM NACL, 2MM CACL2, reverse salting |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.86 (mg/ml) | |
| 2 | 1 | drop | isopropanol | 2.86 (%) | |
| 3 | 1 | drop | ammonium sulfate | 2.0 (M) | |
| 4 | 1 | drop | ethanol | 2.14 (%) | |
| 5 | 1 | reservoir | ethanol | 5 (%) | |
| 6 | 1 | reservoir | ammonium sulfate | 2.1 (M) |
