1KVW
CARBOXYLIC ESTER HYDROLASE, SINGLE MUTANT H48Q OF BOVINE PANCREATIC PLA2 ENZYME
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU R-AXIS II |
| Temperature [K] | 291 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-01-15 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 47.120, 47.120, 102.880 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 1.950 |
| R-factor | 0.209 |
| Rwork | 0.209 |
| R-free | 0.31400 |
| Structure solution method | THE COORDINATES OF THE WILD TYPE (PDB ENTRY 1MKT) WERE USED AS THE STARTING MODEL FOR REFINEMENT. |
| Starting model (for MR) | RECOMBINANT PLA2 (1MKT) |
| RMSD bond length | 0.013 |
| RMSD bond angle | 23.000 * |
| Data reduction software | R-AXIS (IIC) |
| Data scaling software | R-AXIS (II) |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.040 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.082 | 0.218 |
| Total number of observations | 21567 * | |
| Number of reflections | 7424 | |
| Completeness [%] | 73.0 | 50 |
| Redundancy | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.2 | 291 * | CRYSTALS WERE GROWN BY THE VAPOR DIFFUSION METHOD USING THE CONDITIONS 5 (MICRO)L OF THE MUTANT PROTEIN (15MG/ML OF THE PROTEIN), 5MM CACL2, 50MM TRIS BUFFER, PH 7.2 AND 2 (MICRO)L OF 40% MPD AND (60%) OF MPD IN THE RESERVOIR, vapor diffusion |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 11 (mg/ml) | |
| 2 | 1 | drop | Tris | 7.9 (mM) | |
| 3 | 1 | drop | 3.6 (mM) | ||
| 4 | 1 | drop | MPD | 14 (%) | |
| 5 | 1 | reservoir | MPD | 75 (%) |
