1B3K
Plasminogen activator inhibitor-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 111 |
Detector technology | AREA DETECTOR |
Collection date | 1996-09-15 |
Detector | SIEMENS |
Spacegroup name | P 1 |
Unit cell lengths | 65.472, 74.930, 103.691 |
Unit cell angles | 90.97, 93.33, 115.94 |
Refinement procedure
Resolution | 24.350 - 2.990 |
Rwork | 0.247 |
R-free | 0.29200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | LATENT PAI-1 |
RMSD bond length | 0.009 |
RMSD bond angle | 22.100 * |
Data reduction software | BIOMOL |
Data scaling software | X-GEN |
Phasing software | AMoRE |
Refinement software | CNS (0.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.350 | 3.160 |
High resolution limit [Å] | 2.990 | 2.990 |
Rmerge | 0.102 | 0.336 |
Number of reflections | 25373 | |
<I/σ(I)> | 5.11 | 1.03 |
Completeness [%] | 70.7 | 20.3 |
Redundancy | 1.6 | 1.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | CRYSTALS WERE PRODUCED BY THE HANGING DROP METHOD EQUILIBRATING PURIFIED PROTEIN AT 5MG/ML IN 10 MM NA CACODYLATE, PH 6.8, O.25 M NACL, 1 MM EDTA AGAINST 27-32% SATURATED AMMONIUM SULPHATE, 0.25 M NA CL AND 10 MM CACODYLATE PH 6.8 AT ROOM TEMPERATURE, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | SODIUM CACODYLATE | ||
2 | 1 | 1 | NACL | ||
3 | 1 | 1 | EDTA | ||
4 | 1 | 2 | AMMONIUM SULPHATE | ||
5 | 1 | 2 | NACL | ||
6 | 1 | 2 | SODIUM CACODYLATE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 27-32 (%sat) | |
2 | 1 | reservoir | 0.25 (M) | ||
3 | 1 | reservoir | cacodylate | 10 (mM) |