1HSJ
SARR MBP FUSION STRUCTURE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2000-11-12 |
| Spacegroup name | P 1 |
| Unit cell lengths | 64.739, 70.639, 75.473 |
| Unit cell angles | 65.72, 67.18, 69.58 |
Refinement procedure
| Resolution | 19.950 - 2.300 |
| R-factor | 0.2324 * |
| Rwork | 0.263 |
| R-free | 0.28220 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Maltose binding protein 4mbp |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.370 |
| High resolution limit [Å] | 2.280 | 2.280 |
| Rmerge | 0.028 | 0.449 |
| Total number of observations | 77545 * | |
| Number of reflections | 37403 * | |
| <I/σ(I)> | 25.1 | 2.3 |
| Completeness [%] | 96.5 * | 84.8 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | reservoir | beta-mercaptoethanol | 5 (mM) | |
| 3 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 4 | 1 | reservoir | 100 (mM) | ||
| 5 | 1 | reservoir | PEGmme2000 | 18-22 (%) |
