1O8V
The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-02-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 28.714, 54.834, 38.691 |
| Unit cell angles | 90.00, 100.34, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.600 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1PMP CHAIN A |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.100 * | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.043 | 0.066 |
| Total number of observations | 81862 * | |
| Number of reflections | 15644 | |
| <I/σ(I)> | 35 | 14.7 |
| Completeness [%] | 99.8 | 98.6 |
| Redundancy | 5.23 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8.3 * | 30% (V/V) MMEPEG 5000, 0.1 M TRIS-HCL,PH 8.6,0.1 M NAAC. |
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 | 30 (mM) | pH8.3 |
| 3 | 1 | reservoir | PEG5000 MME | 30 (%(v/v)) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.6 |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) |
