1AE5
HUMAN HEPARIN BINDING PROTEIN
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 300 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-09 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 39.190, 66.120, 101.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-free | 0.26600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ppf |
| RMSD bond length | 0.016 |
| RMSD bond angle | 18.430 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.089 | 0.264 |
| Number of reflections | 12176 | |
| <I/σ(I)> | 14.3 | 4.9 |
| Completeness [%] | 99.2 | 98.6 |
| Redundancy | 4.7 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.2 | Iversen, L.F., (1996) Acta Crystallogr.,Sect.D, 52, 1222. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.5 (mg/ml) | |
| 2 | 1 | drop | ethanol | 7-10 (%) | |
| 3 | 1 | drop | glycerol | 2.5-5 (%) | |
| 4 | 1 | drop | Tris-HCl | 0.05 (M) | |
| 5 | 1 | reservoir | ethanol | 14-20 (%) | |
| 6 | 1 | reservoir | glycerol | 5-10 (%) | |
| 7 | 1 | reservoir | Tris-HCl | 0.1 (M) |
