2W2S
Structure of the Lagos bat virus matrix protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 56.870, 56.870, 187.910 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.720 - 2.750 |
| R-factor | 0.21 |
| Rwork | 0.207 |
| R-free | 0.25500 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.093 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | autoSHARP |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.720 | 2.820 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmerge | 0.130 | 0.770 |
| Number of reflections | 5164 | |
| <I/σ(I)> | 10.2 | 2.2 |
| Completeness [%] | 99.6 | 99.4 |
| Redundancy | 6.2 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | SITTING DROPS CONTAINING 100 NL OF 1.1 MG/ML PROTEIN AND 100 NL OF RESERVOIR SOLUTION (100 MM CITRATE PH 4.0 AND 10%(W/V) POLYETHYLENE GLYCOL (PEG) 6000) WERE EQUILIBRATED AGAINST 95 UL RESERVOIRS AT 20.5C. CRYSTALS WERE CRYOPROTECTED BY BRIEF IMMERSION IN RESERVOIR SOLUTION SUPPLEMENTED WITH 25% V/V GLYCEROL. |
