4GF6
crystal structure of GFP with cuprum bound at the Incorporated metal Chelating Amino Acid PYZ151
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2012-03-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.827, 63.052, 70.369 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.100 |
| R-factor | 0.16667 |
| Rwork | 0.166 |
| R-free | 0.17900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ges |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.465 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.140 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.088 | 0.342 |
| Number of reflections | 91616 | |
| <I/σ(I)> | 21.1 | 6.9 |
| Completeness [%] | 99.1 | 99.5 |
| Redundancy | 6.2 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.9 | 289 | 60~100mg/ml protein sample in 50 mM Hepes, pH 7.5, reservior solution:17~19% PEG 3000, 100mM Tris pH 8.9,0.2M calcium acetate , VAPOR DIFFUSION, temperature 289K |
