5L33
Crystal structure of a de novo designed protein with curved beta-sheet
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-01-15 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 28.250, 34.360, 100.390 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.195 - 2.000 |
R-factor | 0.1737 |
Rwork | 0.172 |
R-free | 0.20130 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.875 |
Data reduction software | iMOSFLM (7.1.0) |
Data scaling software | Aimless (0.2.8) |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX (dev_1616) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.195 |
High resolution limit [Å] | 2.000 |
Number of reflections | 6503 |
<I/σ(I)> | 24.6 |
Completeness [%] | 92.3 |
Redundancy | 7.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.1 M sodium MOPS/HEPES, pH 7.5, 12.5% PEG 1000, 12.5% PEG 3350 and 12.5% 2-methyl-2,4-pentanediol and 0.2 M of amino acids (sodium glutamate, DL-alanine, glycine, DL-lysine HCl and DL-serine) |