1SCR
HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE CO,CA-PROTEIN AT 1.6 ANGSTROMS AND THE NI,CA-PROTEIN AT 2.0 ANGSTROMS
Experimental procedure
Spacegroup name | I 2 2 2 |
Unit cell lengths | 89.440, 87.210, 63.060 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.159 |
Rwork | 0.159 |
RMSD bond length | 0.013 |
RMSD bond angle | 2.800 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.000 * |
Rmerge | 0.040 * |
Total number of observations | 60304 * |
Number of reflections | 16435 * |
Completeness [%] | 97.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 6.5 * | Greer, J., (1970) J. Mol. Biol, 48, 365. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | 0.1 (M) | ||
2 | 1 | 1 | Tris acetate | 0.05 (M) |