4GES
crystal structure of GFP-TYR151PYZ with an unnatural amino acid incorporation
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 | 2012-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.717, 50.809, 62.364 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.870 - 1.230 |
R-factor | 0.16414 |
Rwork | 0.163 |
R-free | 0.18773 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gfl |
RMSD bond length | 0.009 |
RMSD bond angle | 1.474 |
Data reduction software | DENZO |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.230 |
Rmerge | 0.090 |
Number of reflections | 62551 |
<I/σ(I)> | 23.5 |
Completeness [%] | 98.7 |
Redundancy | 9.5 |
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:16~19% PEG 3000, 100mM Tris pH 8.9,0.2M calcium acetate, VAPOR DIFFUSION, temperature 289K |