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) |






