3HNU
Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG in P21 space group
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-16 |
| Detector | RIGAKU SATURN 944 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.876, 34.444, 45.632 |
| Unit cell angles | 90.00, 101.24, 90.00 |
Refinement procedure
| Resolution | 24.490 - 1.560 |
| R-factor | 0.187 |
| Rwork | 0.183 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PSEUDO-MONOMERIC CV-N (1M5M) |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.141 |
| 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] | 24.490 | 1.620 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.047 | 0.175 |
| Number of reflections | 14212 | |
| <I/σ(I)> | 19.9 | 3.2 |
| Completeness [%] | 95.5 | 71.4 |
| Redundancy | 3.9 | 2.21 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 277 | 40 mg/ml protein in 0.2 M Li2SO4, 0.1 M Tris-HCl (pH 8.5), and 30% PEG 4000 at 8 to 1 ratio between protein and mother liquor, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
