2HPC
Crystal structure of fragment D from Human Fibrinogen Complexed with Gly-Pro-Arg-Pro-amide.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-03-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.95 |
Spacegroup name | P 1 2 1 |
Unit cell lengths | 81.677, 46.069, 429.901 |
Unit cell angles | 90.00, 89.99, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.900 |
R-factor | 0.2792 |
Rwork | 0.275 |
R-free | 0.36020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hod |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.600 |
Number of reflections | 91090 |
Completeness [%] | 88.9 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | equal volumes of 10 mg/ml fragment D, 5 mM Gly-Pro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0, 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |