1BFF
THE 154 AMINO ACID FORM OF HUMAN BASIC FIBROBLAST GROWTH FACTOR
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 293 |
| Detector technology | AREA DETECTOR |
| Collection date | 1991-07 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | P 1 |
| Unit cell lengths | 30.800, 33.300, 36.500 |
| Unit cell angles | 64.10, 73.00, 76.10 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.19 * |
| Rwork | 0.190 |
| Structure solution method | DIFFERENCE FOURIER |
| Starting model (for MR) | 4fgf |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.700 |
| Data reduction software | XUONG-HAMLIN ((DETECTOR SYSTEM)) |
| Data scaling software | XUONG-HAMLIN ((DETECTOR SYSTEM)) |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.043 * | |
| Total number of observations | 15506 * | |
| Number of reflections | 7035 | |
| <I/σ(I)> | 9.3 | 2.1 |
| Completeness [%] | 84.0 | 46 |
| Redundancy | 2.2 | 1.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | THE PROTEIN WAS CRYSTALLIZED FROM 30-40 % PEG1000 AND 0.2-0.3 % 2-MERCAPTOETHANOL BY THE HANGING DROP VAPOR DIFFUSION METHOD., pH 7.5, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | hbFGF154 | 0.003-0.005ml | |
| 2 | 1 | drop | PEG1000 | 15-20 (%) | |
| 3 | 1 | drop | beta-mercaptoethanol | 0.1-0.15 (%) | |
| 4 | 1 | reservoir | PEG1000 | 30-40 (%) | |
| 5 | 1 | reservoir | beta-mercaptoethanol | 0.2-0.3 (%) |
