3LRH
Structure of anti-huntingtin VL domain in complex with huntingtin peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-11-03 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.090, 89.660, 95.000 |
Unit cell angles | 90.00, 99.45, 90.00 |
Refinement procedure
Resolution | 19.860 - 2.600 |
R-factor | 0.21885 |
Rwork | 0.216 |
R-free | 0.27804 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3lrg |
RMSD bond length | 0.005 |
RMSD bond angle | 0.828 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.700 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.114 | 0.318 |
Number of reflections | 24090 | |
<I/σ(I)> | 9.8 | 4.1 |
Completeness [%] | 88.7 | 92 |
Redundancy | 2.8 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.1 | 293 | 10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |