1FZA
CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 297 |
Collection date | 1996-02 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 107.720, 48.080, 167.560 |
Unit cell angles | 90.00, 105.70, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.900 |
R-factor | 0.263 |
Rwork | 0.263 |
R-free | 0.36300 |
Structure solution method | ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.630 |
Phasing software | PHASES |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.900 |
Rmerge | 0.145 |
Total number of observations | 318238 * |
Number of reflections | 35552 |
Completeness [%] | 87.1 |
Redundancy | 8.95 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | SYMMETRY OPERATIONS FOR NON-STANDARD SETTING: X, Y, Z -X, Y+1/2, -Z |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3350 | 16-19 (%) | |
2 | 1 | reservoir | Tris-HCl | 50 (mM) | |
3 | 1 | reservoir | 2 (mM) | ||
4 | 1 | reservoir | 50-133 (mM) |