1IAM
STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 1995-02-26 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 41.857, 124.736, 83.186 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 - 2.100 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.30300 |
Structure solution method | MOLECULAR REPLACEMENT, MIR, PHASE RECOMBINATION |
Starting model (for MR) | ICAM-2 PDB ENTRY 1ZXQ |
RMSD bond length | 0.009 |
RMSD bond angle | 28.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.036 | 0.059 |
Number of reflections | 10629 | |
<I/σ(I)> | 24.15 | 10.21 |
Completeness [%] | 81.1 | 33.4 |
Redundancy | 3 | 0.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | PROTEIN IN 10 MM TRIS, PH 7.5, 25 MM NACL, WAS CRYSTALLIZED FROM 20% PEG 4000 IN 10 MM TRIS AS PRECIPITANT |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris | 10 (mM) | |
3 | 1 | drop | 25 (mM) | ||
4 | 1 | reservoir | PEG4000 | 20 (%) | |
5 | 1 | reservoir | Tris | 10 (mM) |