3HUS
Crystal structure of recombinant gamma N308K fibrinogen fragment D with the peptide ligand Gly-Pro-Arg-Pro-amide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-04-22 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.99000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 95.009, 95.009, 448.382 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.250 - 3.040 |
R-factor | 0.23768 |
Rwork | 0.220 |
R-free | 0.28802 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ltj |
RMSD bond length | 0.007 |
RMSD bond angle | 1.039 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 47.250 |
High resolution limit [Å] | 3.040 |
Number of reflections | 40798 |
Completeness [%] | 99.4 |
Redundancy | 8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 9% PEG 3350, 50 mM Tris-HCl pH 8.5, 2 mM Sodium azide, 12.5 mM Calcium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 277K |