1AIC
STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHOSPHATE BINDING LYSINE RESIDUE
Experimental procedure
Spacegroup name | P 1 21 1 |
Unit cell lengths | 87.200, 79.900, 89.600 |
Unit cell angles | 90.00, 119.10, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.400 |
R-factor | 0.191 |
Rwork | 0.191 |
RMSD bond length | 0.013 |
RMSD bond angle | 3.120 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 10.000 * |
High resolution limit [Å] | 2.400 * |
Rmerge | 0.047 * |
Number of reflections | 72346 * |
Completeness [%] | 93.1 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15.1 (mg/mL) | |
2 | 1 | drop | maleate | 100 (mM) | |
3 | 1 | drop | sodium chloride | 0.45-0.55 (M) | |
4 | 1 | drop | PEG | 16 (%(w/v)) | |
5 | 1 | drop | sodium phosphate | 20 (mM) | |
6 | 1 | reservoir | PEG | 32 (%(w/v)) | |
7 | 1 | reservoir | sodium chloride | 0.9-1.1 (M) | |
8 | 1 | reservoir | sodium phosphate | 20 (mM) |