2EVT
Crystal structure of D48V mutant of human Glycolipid Transfer Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 2004-07-20 |
Detector | RIGAKU RAXIS HTC |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.459, 35.360, 58.011 |
Unit cell angles | 90.00, 116.47, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.990 |
R-factor | 0.203 |
Rwork | 0.201 |
R-free | 0.25500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1swx |
RMSD bond length | 0.010 |
RMSD bond angle | 1.120 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 1.990 | 1.990 |
Rmerge | 0.104 | 0.498 |
Number of reflections | 13588 | |
<I/σ(I)> | 18.7 | |
Completeness [%] | 98.1 | 94.6 |
Redundancy | 3.5 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | PEG, potassium phosphate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |