1AOA
N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1995-08 |
Detector | SIEMENS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.032, 61.241, 102.298 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.400 |
R-factor | 0.186 |
Rwork | 0.186 |
R-free | 0.28500 |
Structure solution method | MIR |
RMSD bond length | 0.011 |
RMSD bond angle | 22.690 * |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASES |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.059 | 0.217 |
Total number of observations | 39834 * | |
Number of reflections | 11764 | |
Completeness [%] | 80.0 | 77.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * | 4 * | PROTEIN WAS CRYSTALLIZED FROM 8-20: PEG 8000, 20 MM CALCIUM ACETATE, 100MM SODIUM CACODYLATE, PH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | PIPES | 10 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | 1 (mM) | ||
5 | 1 | drop | EGTA | 0.1 (mM) | |
6 | 1 | drop | dithiothreitol | 1 (mM) | |
7 | 1 | reservoir | PEG8000 | 8-20 (%) | |
8 | 1 | reservoir | calcium acetate | 20 (mM) | |
9 | 1 | reservoir | sodium cacodylate | 100 (mM) |