1KV0
Cis/trans Isomerization of Non-prolyl Peptide Bond Observed in Crystal Structure of an Scorpion Toxin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-18B |
| Synchrotron site | Photon Factory |
| Beamline | BL-18B |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2000-12-24 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 32.758, 32.758, 176.822 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.300 * - 1.400 |
| R-factor | 0.14416 |
| Rwork | 0.142 |
| R-free | 0.16400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sn1 |
| RMSD bond length | 0.017 * |
| RMSD bond angle | 1.983 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.04) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.300 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.040 | 0.201 |
| Total number of observations | 57131 * | |
| Number of reflections | 19260 | |
| <I/σ(I)> | 3.6 | |
| Completeness [%] | 85.8 | 74.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | ammonium sulfate, Tris-HCl, Ethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.65 (M) | |
| 3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5 |
| 4 | 1 | reservoir | ethanol | 1 (%(v/v)) |
