1FNH
CRYSTAL STRUCTURE OF HEPARIN AND INTEGRIN BINDING SEGMENT OF HUMAN FIBRONECTIN
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-11 |
Detector | MARRESEARCH |
Wavelength(s) | .9787, .9788, .9115, .9796 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 68.580, 86.290, 142.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.800 |
R-factor | 0.216 * |
Rwork | 0.216 |
R-free | 0.29500 |
Structure solution method | MAD |
RMSD bond length | 0.014 |
RMSD bond angle | 26.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 3.620 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.080 | 0.270 |
Number of reflections | 5479 | |
<I/σ(I)> | 14 | 6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 20 * | protein solution is mixed in a 1:1 ratio with well solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4-6 (mg/ml) | |
2 | 1 | reservoir | HEPES | 0.1 (mM) | |
3 | 1 | reservoir | Na, K Tartrate | 0.8 (M) |