1HPC
REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE
Experimental procedure
Spacegroup name | P 31 2 1 |
Unit cell lengths | 57.300, 57.300, 136.800 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.185 |
Rwork | 0.185 |
RMSD bond length | 0.011 |
RMSD bond angle | 2.800 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
High resolution limit [Å] | 2.000 * | 2.000 * |
Rmerge | 0.081 * | |
Total number of observations | 87067 * | |
Number of reflections | 17031 | |
Completeness [%] | 92.0 | 80 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 5.2 * | 281 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | ammonium sulfate | 2 (M) | |
2 | 1 | 2 | Tris naleate | 0.1 (M) |