2FWW
human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 113 |
Detector technology | CCD |
Collection date | 2004-06-19 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 31 |
Unit cell lengths | 77.920, 77.920, 164.030 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.250 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.25700 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.007 |
RMSD bond angle | 1.450 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.290 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.081 | |
Number of reflections | 52849 | |
Completeness [%] | 99.9 | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 293 | 2mg/mL of protein, 10 mM MES, pH 6.1, 2M NaCl was mixed with crystallization solution 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, 30% PEG 1500. Crystallization drops were set up using various ratios of protein solution to crystallization solution. Crystals appropriate for diffraction studies appeared in 2-5 days at room temperature, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |