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) |