3BKD
High resolution Crystal structure of Transmembrane domain of M2 protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-10-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97853 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.753, 56.557, 56.009 |
| Unit cell angles | 90.00, 103.53, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.050 |
| R-factor | 0.22158 |
| Rwork | 0.219 |
| R-free | 0.26871 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Amantandine-bound M2TM; G34A mutant |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.348 |
| 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] | 50.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.062 | 0.305 |
| Number of reflections | 14567 | |
| <I/σ(I)> | 22.4 | 1.9 |
| Completeness [%] | 94.9 | 75.1 |
| Redundancy | 3.4 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 298 | Protein solution: 0.8mM protein, 32mM n-octyl-beta-D-glucopyranoside and 5%v/v xylitol. Reservoir solution: 50mM Tris-Hcl, 500mM MgCl2, 21% PEG 350 MME, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
