1JOH
THE STRUCTURE OF ANTIAMOEBIN I, A MEMBRANE-ACTIVE PEPTIDE
Experimental procedure
| Source type | SEALED TUBE |
| Temperature [K] | 293 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1986 |
| Detector | HILGER-WATTS |
| Spacegroup name | P 1 |
| Unit cell lengths | 26.530, 28.820, 9.060 |
| Unit cell angles | 88.90, 96.64, 123.85 |
Refinement procedure
| Resolution | 25.000 - 1.400 |
| R-factor | 0.156 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | RESIDUES 6 - 16 OF LEU1-ZERVAMICIN WITH ALL NON -EQUIVALENT SIDE-CHAINS TRIMMED TO ALA. |
| RMSD bond length | 0.036 |
| RMSD bond angle | 3.152 |
| Phasing software | SHELXL-93 |
| Refinement software | SHELXL-93 |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.000 |
| High resolution limit [Å] | 1.200 |
| Rmerge | 0.012 |
| Number of reflections | 6715 |
| <I/σ(I)> | 10.5 |
| Completeness [%] | 93.7 |
| Redundancy | 1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | peptide | 170 (mg/ml) |
