3LBW
High resolution crystal structure of transmembrane domain of M2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-25 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.91910 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 48.665, 79.091, 48.559 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.530 - 1.650 |
| R-factor | 0.19664 |
| Rwork | 0.196 |
| R-free | 0.20529 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bkd chain A |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.866 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.560 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.070 | 0.447 |
| Number of reflections | 11509 | |
| <I/σ(I)> | 19.4 | 2.7 |
| Completeness [%] | 99.5 | 96.6 |
| Redundancy | 6.6 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | Protein solution: 0.8mM M2TM (25-46) peptide (as monomer),28mM Octyl-beta-D-Glucopyranosie and 5% xylitol. Reservoir solution: 95% [100mM sodium citrate pH 5.6, 150mM tri-sodium citrate, 15% v/v isopropanol] and 5% [0.2M MgCl2 6H20, 0.1M Tris-Hcl pH 8.5, 30% w/v PEG 4000], VAPOR DIFFUSION, HANGING DROP |
