3EE6
Crystal Structure Analysis of Tripeptidyl peptidase -I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-03-20 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 113.450, 128.930, 100.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.210 - 2.350 |
R-factor | 0.221 |
Rwork | 0.218 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.436 |
Data reduction software | HKL-2000 |
Data scaling software | SADABS |
Phasing software | SHELXD |
Refinement software | REFMAC (5.4.0069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.210 | 2.450 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.034 | 0.312 |
Number of reflections | 61321 | |
<I/σ(I)> | 17.2 | 3.15 |
Completeness [%] | 98.8 | 97.2 |
Redundancy | 7.18 | 6.11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 4.9 | 293 | 7% PEG 4000, 0.02M zinc sulfate, 0.1M sodium acetate, 0.1M ammonium sulfate, pH 4.9, VAPOR DIFFUSION, temperature 293K |