1FGA
REFINEMENT OF THE STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION AND ANALYSIS OF PRESUMED HEPARIN BINDING SITES BY SELENATE SUBSTITUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | rotating-anode X-ray tube |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Detector | AREA DETECTOR |
| Spacegroup name | P 1 |
| Unit cell lengths | 30.800, 33.500, 35.800 |
| Unit cell angles | 58.80, 72.40, 76.10 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.138 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 3.200 |
| Data scaling software | Xengen (HOWARD, NIELSEN, XUONG) |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 2.200 * |
| High resolution limit [Å] | 1.600 * |
| Rmerge | 0.040 * |
| Number of reflections | 13971 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8.1 * | using macroseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 2 | ammonium sulfate | 2.0 (M) | |
| 2 | 1 | 2 | Tris-HCl | 0.1 (M) | |
| 3 | 1 | 2 | 0.1 (M) | ||
| 4 | 1 | 2 | BME | 0.1 (%(v/v)) |






