3HP8
Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG, bound to sucrose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-05-10 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.497, 39.298, 86.134 |
| Unit cell angles | 90.00, 97.64, 90.00 |
Refinement procedure
| Resolution | 35.700 - 2.000 |
| R-factor | 0.227 |
| Rwork | 0.224 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hnu |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.596 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.700 | 1.950 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.166 | 0.413 |
| Number of reflections | 23572 | |
| <I/σ(I)> | 3.9 | 1.4 |
| Completeness [%] | 96.7 | 76.1 |
| Redundancy | 3.08 | 2.92 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 277 | protein solutions (~40 mg/ml) were incubated overnight with sucrose at a molar ratio of 1:40 (protein:disaccharide) and crystallization were carried out using 0.2 M Li2SO4, 0.1 M Tris-HCl (pH 8.5), and 30% PEG 4000 with protein to mother liquor ratio of 8 to 1 , VAPOR DIFFUSION, SITTING DROP, temperature 277K |
