1LTO
Human alpha1-tryptase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 91.441, 110.685, 130.092 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.940 - 2.200 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.26000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HUMAN B-TRYPTASE |
RMSD bond length | 0.010 |
RMSD bond angle | 1.700 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.940 * | 2.330 |
High resolution limit [Å] | 2.200 * | 2.190 |
Rmerge | 0.066 * | 0.349 * |
Number of reflections | 64252 | |
<I/σ(I)> | 7.7 | |
Completeness [%] | 94.7 * | 71.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.6 * | 293 | PEG 4K, MgAc, MES, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6.6 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 22 (%(w/v)) | |
3 | 1 | reservoir | 0.1 (M) | ||
4 | 1 | reservoir | HEPES | 100 (mM) | pH7.6 |