4KGS
Backbone Modifications in the Protein GB1 Loops: beta-3-Val21, beta-3-Asp40
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-04-06 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 80.657, 35.660, 46.531 |
Unit cell angles | 90.00, 120.44, 90.00 |
Refinement procedure
Resolution | 28.269 - 1.950 |
R-factor | 0.1759 |
Rwork | 0.174 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB 2QMT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.116 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.270 |
High resolution limit [Å] | 1.950 |
Rmerge | 0.078 |
Number of reflections | 8453 |
<I/σ(I)> | 7.8 |
Completeness [%] | 99.6 |
Redundancy | 6.08 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 0.1 M sodium acetate pH 4.6, 16% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K |