1GZY
Human Insulin-like growth factor; In-house data
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 30.723, 69.282, 64.528 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.000 * - 2.540 |
| R-factor | 0.218 |
| Rwork | 0.213 |
| R-free | 0.27200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ins |
| RMSD bond length | 0.013 * |
| RMSD bond angle | 1.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.000 * | 2.070 |
| High resolution limit [Å] | 2.540 * | 2.540 * |
| Rmerge | 0.086 * | 0.331 * |
| Total number of observations | 8654 * | |
| Number of reflections | 2065 * | |
| <I/σ(I)> | 18 | 12 |
| Completeness [%] | 98.1 * | 95 * |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7 (mg/ml) | in water |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH7.5 |
| 3 | 1 | reservoir | PEG2000MME | 12-15 (%(w/v)) | |
| 4 | 1 | reservoir | SB12 detergent | 5 (mM) |






