1TIC
CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR
Experimental procedure
Spacegroup name | C 1 21 1 |
Unit cell lengths | 92.770, 128.860, 78.350 |
Unit cell angles | 90.00, 135.82, 90.00 |
Refinement procedure
Resolution | 7.500 - 2.600 |
R-factor | 0.16 |
RMSD bond length | 0.016 |
RMSD bond angle | 0.056 |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.600 * |
Rmerge | 0.088 * |
Completeness [%] | 87.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 1.2 (%) | |
2 | 1 | reservoir | ammonium sulfate | 40 (%) | |
3 | 1 | reservoir | sodium acetate | 100 (mM) | |
4 | 1 | reservoir | MPD | 0.020ml | |
5 | 1 | reservoir | N,N-dimethyl-octadecylamine-N-oxide | 0.05 (mM) |