2G2S
Structure of S65G Y66S GFP variant after spontaneous peptide hydrolysis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-01-20 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.000, 62.300, 68.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.800 - 1.200 |
R-free | 0.17400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ema |
RMSD bond length | 0.014 |
RMSD bond angle | 0.029 |
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] | 17.800 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Number of reflections | 68670 | |
<I/σ(I)> | 44 | 5.1 |
Completeness [%] | 99.3 | 94.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 298 | 50 mM MgCl2, 50 mM Hepes, 20% PEG 4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 8.00 |