1LTJ
Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-11-09 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.284, 94.218, 226.936 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.000 * - 2.800 |
| Rwork | 0.212 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fzc |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.280 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.123 * | 0.393 * |
| Total number of observations | 181953 * | |
| Number of reflections | 46717 | |
| <I/σ(I)> | 13.8 | 2.9 |
| Completeness [%] | 97.8 | 92.8 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 * | 4 * | 7% PEG 3350, 12.5mM Calcium Chloride, 2mM Sodium Azide, 50mM Tris pH 8.5, 2mM GHRP-amide, 2mM GPRP-amide, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | pH7.0 |
| 3 | 1 | drop | GHRPam | 2 (mM) | |
| 4 | 1 | drop | GPRPam | 2 (mM) | |
| 5 | 1 | reservoir | Tris | 50 (mM) | pH8.5 |
| 6 | 1 | reservoir | 2 (mM) | ||
| 7 | 1 | reservoir | 12.5 (mM) | ||
| 8 | 1 | reservoir | PEG3350 | 7 (%) |
