1FUN
SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)
Experimental procedure
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 287 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 205.200, 167.000, 145.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.850 |
R-factor | 0.189 |
Rwork | 0.189 |
R-free | 0.25700 * |
Structure solution method | OTHER |
RMSD bond length | 0.017 |
RMSD bond angle | 1.700 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 99.000 |
High resolution limit [Å] | 2.850 |
Rmerge | 0.105 |
Number of reflections | 58307 |
Completeness [%] | 99.6 |
Redundancy | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.7 * | Parge, H.E., (1986) J. Biol. Chem., 261, 16215. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | potassium phosphate | 50 (mM) | |
2 | 1 | drop | protein | 2 (%(w/v)) | |
3 | 1 | reservoir | Tris-HCl | 50 (mM) | |
4 | 1 | reservoir | 50 (mM) | ||
5 | 1 | reservoir | EDTA | 0.1 (mM) | |
6 | 1 | reservoir | 0.01 (%) |