219L
PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME
Experimental procedure
Detector technology | AREA DETECTOR |
Collection date | 1994-10-16 |
Detector | XUONG-HAMLIN MULTIWIRE |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 60.580, 60.580, 97.470 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.230 - 1.660 |
R-factor | 0.175 * |
Rwork | 0.175 |
RMSD bond length | 0.014 |
RMSD bond angle | 2.070 |
Data reduction software | UCSD |
Refinement software | TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 26.230 |
High resolution limit [Å] | 1.660 |
Rmerge | 0.068 |
Number of reflections | 21597 |
Completeness [%] | 87.9 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 7.1 * | MUTANT WAS CRYSTALLIZED FROM PHOSPHATE IN CONTRAST TO L1 64AAA_PEG WHICH WAS CRYSTALLIZED FROM PEG. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | phosphate | 2.2 (M) | |
2 | 1 | 1 | 0.25 (M) | ||
3 | 1 | 1 | beta-mercaptoethanol | 50 (mM) | reduced |
4 | 1 | 1 | dioxane | 0.25 (%(v/v)) |