2DSN
Crystal structure of T1 lipase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 117.731, 81.270, 99.912 |
Unit cell angles | 90.00, 97.09, 90.00 |
Refinement procedure
Resolution | 40.330 - 1.500 |
R-factor | 0.174 |
Rwork | 0.174 |
R-free | 0.18800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ji3 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.330 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.057 | 0.321 |
Number of reflections | 140733 | |
<I/σ(I)> | 12.4 | 2.3 |
Completeness [%] | 94.7 | 85.1 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 293 | 0.5M NaCl, 0.1M KH2PO4, 0.1M NaH2PO4, 0.1M MES buffer, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |