1JOJ
CONCANAVALIN A-HEXAPEPTIDE COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Detector technology | IMAGE PLATE |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 102.685, 118.384, 253.593 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 3.000 |
| R-factor | 0.186 * |
| Rwork | 0.186 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5cna |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.800 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 3.130 | |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.101 | 0.257 * |
| Number of reflections | 23957 | |
| <I/σ(I)> | 10.6 | 5.37 |
| Completeness [%] | 78.1 | 71.8 |
| Redundancy | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 0.32 (mM) | |
| 2 | 1 | drop | peptide | 20-fold molar excess | |
| 3 | 1 | reservoir | ammonium sulfate | pH9.0 | |
| 4 | 1 | reservoir | Tris | 50 (mM) |
