1QFK
STRUCTURE OF HUMAN FACTOR VIIA AND ITS IMPLICATIONS FOR THE TRIGGERING OF BLOOD COAGULATION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-05 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 115.300, 115.300, 98.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.000 - 2.800 |
| R-factor | 0.215 * |
| Rwork | 0.215 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dan |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.045 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.056 * | 0.253 |
| Total number of observations | 238127 * | |
| Number of reflections | 16157 | |
| <I/σ(I)> | 15.4 | 3 |
| Completeness [%] | 95.4 | 79.4 |
| Redundancy | 4.0 * | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 50MM NACL, 10MM CACL2, 3.5-3.7M SODIUM FORMATE IN 100MM TRIS PH 8.5, pH 8.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12-20 (mg/ml) | |
| 2 | 1 | drop | 50 (mM) | ||
| 3 | 1 | drop | Tris | 10 (mM) | |
| 4 | 1 | reservoir | 50 (mM) | ||
| 5 | 1 | reservoir | 10 (mM) | ||
| 6 | 1 | reservoir | sodium formate | 3.5-3.7 (M) | |
| 7 | 1 | reservoir | Tris | 100 (mM) |
