2Y6V
Peroxisomal alpha-beta-hydrolase Lpx1 (Yor084w) from Saccharomyces cerevisiae (crystal form I)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-09-03 |
| Detector | RIGAKU CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 140.480, 87.770, 125.040 |
| Unit cell angles | 90.00, 95.10, 90.00 |
Refinement procedure
| Resolution | 19.750 - 2.830 |
| R-factor | 0.20938 |
| Rwork | 0.207 |
| R-free | 0.25408 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ENSEMBLE OF TEN ALPHA-BETA HYDROLASES AS POLY-ALA MODELS TRIMMED TO THE COMMON CORE. |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.475 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.900 |
| High resolution limit [Å] | 2.830 | 2.830 |
| Rmerge | 0.090 | 0.400 |
| Number of reflections | 34876 | |
| <I/σ(I)> | 15 | 2.97 |
| Completeness [%] | 95.6 | 68.4 |
| Redundancy | 3.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | HANGING OR SITTING DROP VAPOR DIFFUSION AT 20 DEGREES CELSIUS. 4 UL OF PROTEIN (7.9 MG/ML) MIXED WITH 2UL RESERVOIR (0.1 M HEPES, PH 7.5, 10 % PEG 8000). |






