1HTP
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 COMPLEX
Experimental procedure
Spacegroup name | P 21 21 2 |
Unit cell lengths | 61.340, 55.380, 33.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.185 |
Rwork | 0.185 |
RMSD bond length | 0.014 |
RMSD bond angle | 2.900 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.200 * |
Rmerge | 0.054 * |
Total number of observations | 14236 * |
Number of reflections | 5684 |
Completeness [%] | 91.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 5.2 * | 8 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | H-Proox | 7-14 (mg/ml) | can be replaced with 3-5mg/ml H-ProMet |
2 | 1 | drop | TrisMaleate | 0.1 (M) | |
3 | 1 | reservoir | ammonium sulfate | 2 (M) |