1JMY
Truncated Recombinant Human Bile Salt Stimulated Lipase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 113 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.640, 90.080, 103.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 - 2.600 |
| R-factor | 0.236 * |
| Rwork | 0.236 |
| R-free | 0.27600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Truncated core of acetylcholinesterase |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 1.490 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.100 | 0.350 |
| Number of reflections | 15613 | |
| <I/σ(I)> | 6.3 | 2 |
| Completeness [%] | 90.7 * | 74.9 |
| Redundancy | 3.2 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3 * | 293 | Kingston, R.L., (2000) Acta Crystallogr., Sect.D, 56, 478. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 0.5-0.8 (mg/ml) | |
| 2 | 1 | drop | MOPS-NH4OH | 20 (mM) | |
| 3 | 1 | drop | 0.1 (M) | ||
| 4 | 1 | drop | CHAPS | 0.8 (mM) | |
| 5 | 1 | reservoir | PIPES-KOH | 0.2 (M) | |
| 6 | 1 | reservoir | PEG6000 | 15-25 (%) | |
| 7 | 1 | reservoir | glycerol | 2 (%) |
