1QK8
TRYPAREDOXIN-I FROM CRITHIDIA FASCICULATA
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-11-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.88, 0.97 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.390, 50.700, 70.820 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.400 |
| Rwork | 0.191 |
| R-free | 0.22300 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.030 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.000 | 1.430 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.029 | 0.170 |
| Number of reflections | 49768 | |
| <I/σ(I)> | 145.1 | 103.1 |
| Completeness [%] | 94.5 | 65.6 |
| Redundancy | 2 | 1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.4 * | 4 * | 6.75MG/ML PROTEIN, 7.5% PEG MME 2000, 0.025M TRIS/HCL PH8.2, 0.25% DMSO, pH 7.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | reservoir | Tris-HCl | 50-100 (mM) | |
| 4 | 1 | reservoir | 80 (mM) | ||
| 5 | 1 | reservoir | PEG8000 | 17-20 (%) |
