1HLG
CRYSTAL STRUCTURE OF HUMAN GASTRIC LIPASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE DW32 |
Synchrotron site | LURE |
Beamline | DW32 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-09 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | I 21 3 |
Unit cell lengths | 244.330, 244.330, 244.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.000 |
Rwork | 0.210 |
R-free | 0.22800 |
Structure solution method | SIRAS |
RMSD bond length | 0.007 |
RMSD bond angle | 24.200 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | X-PLOR (3843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 3.100 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.068 | 0.399 |
Number of reflections | 45522 | |
<I/σ(I)> | 10.9 | 2 |
Completeness [%] | 99.6 | 100 |
Redundancy | 4 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-6 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2 (M) | |
3 | 1 | reservoir | tert-butanol | 1.4 (%) |