1B4W
BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 280 |
| Detector technology | AREA DETECTOR |
| Collection date | 1997-08-15 |
| Detector | SIEMENS |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 100.453, 54.294, 108.388 |
| Unit cell angles | 90.00, 111.76, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.600 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.28600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pp2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 26.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.102 | 0.381 |
| Total number of observations | 42427 * | |
| Number of reflections | 16462 | |
| <I/σ(I)> | 10.4 | 2.6 |
| Completeness [%] | 97.3 | 93.1 * |
| Redundancy | 2.6 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8.5 | THE PROTEIN SOLUTIONS CONTAINED 0.1M LI2SO4, 9% PEG 4K AND 0.3% N-OCTYL BETA- D-GLUCOPYRANOSIDE IN 0.01M TRIS-HCL BUFFER(PH 8.5) AND AN ENZYME CONCENTRATION OF 8MG/ML; THE SOLUTION IN RESERVOIR CONTAINED 18% PEG 4K IN SAME BUFFER, ROOM TEMPERATURE OF 17DEG.C. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | PEG4000 | 8 (%(w/v)) | |
| 3 | 1 | drop | Tris-HCl | 0.1 (M) | |
| 4 | 1 | drop | 0.1 (M) | ||
| 5 | 1 | drop | beta-OG | 0.3 (%) | |
| 6 | 1 | reservoir | PEG4000 | 16 (%(v/v)) |
