1PLU
PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 291 |
| Detector technology | AREA DETECTOR |
| Collection date | 1992-06 |
| Detector | SDMS |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.600, 80.600, 95.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PREVIOUS PELC MODEL |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.190 * |
| Data reduction software | SDMS (SOFTWARE) |
| Data scaling software | SDMS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 |
| High resolution limit [Å] | 2.200 |
| Number of reflections | 24983 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.9 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 1.0MM LUCL3, 1.0M AMMONIUM SULFATE, AND 50MM HEPES, PH 6.9 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (A280/ml) | |
| 2 | 1 | drop | 1.0 (M) | ||
| 3 | 1 | drop | HEPES | 50 (mM) | |
| 4 | 1 | drop | 1 (mM) | ||
| 5 | 1 | reservoir | 2.0 (M) | ||
| 6 | 1 | reservoir | HEPES | 0.1 (M) |
