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 |