2G5Z
Structure of S65G Y66S GFP variant after spontaneous peptide hydrolysis and decarboxylation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-04 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97946 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.070, 62.570, 71.650 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
Rwork | 0.160 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ema |
RMSD bond length | 0.007 |
RMSD bond angle | 0.024 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 21833 | |
<I/σ(I)> | 28.8 | 6.4 |
Completeness [%] | 100.0 | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 50 mM MgCl2, 50 mM Hepes, 20% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 8.0 |