3EDY
Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4C |
Synchrotron site | NSLS |
Beamline | X4C |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-10-02 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 0.97908 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.807, 93.173, 102.479 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.720 - 1.850 |
R-factor | 0.179 |
Rwork | 0.179 |
R-free | 0.20500 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.263 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.900 |
High resolution limit [Å] | 1.830 | 1.830 |
Rmerge | 0.079 | 0.457 |
Number of reflections | 50890 | |
<I/σ(I)> | 2.3 | |
Completeness [%] | 99.1 | 93.1 |
Redundancy | 7 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 278 | PEG 6000, citrate, pH 5.0, vapor diffusion, hanging drop, temperature 278K |