1PLC
ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN AT 1.33 ANGSTROMS RESOLUTION
Replaces: 1PCYExperimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 29.600, 46.860, 57.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.330 |
| R-factor | 0.15 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.032 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.330 * |
| Rmerge | 0.100 * |
| Total number of observations | 14512 * |
| Number of reflections | 8460 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6 * | taken from Chapman, G.V. et al (1977). J. Mol. Biol., 110, 187-189. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-10 (mg/ml) | |
| 2 | 1 | reservoir | sodium phosphate | 0.1 (M) | |
| 3 | 1 | reservoir | ammonium sulfate | 2.6 (M) |
