3C9J
The Crystal structure of Transmembrane domain of M2 protein and Amantadine complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-12-08 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 60.397, 57.833, 38.105 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.500 |
R-factor | 0.29322 |
Rwork | 0.291 |
R-free | 0.31668 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Polyala single alpha helix of length 23 residues |
RMSD bond length | 0.029 |
RMSD bond angle | 2.165 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 3.610 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.105 | 0.362 |
Number of reflections | 1848 | |
<I/σ(I)> | 12.3 | 3.1 |
Completeness [%] | 92.4 | 100 |
Redundancy | 4.2 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.3 | 298 | Sample solution: 0.8mM protein, 0.6mM Amantadine, 32mM n-octyl-beta-D-glucopyranoside and 5% w/v Xylitol. Reservoir solution:50mM Tris-Hcl, 500mM MgCl2, 30mM NiCl2, 22% PEG 350 MME, pH 5.3, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |