1URA
ALKALINE PHOSPHATASE (D51ZN)
Experimental procedure
Collection date | 1994-06-29 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 194.810, 166.870, 76.390 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.040 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.23400 |
RMSD bond length | 0.020 |
RMSD bond angle | 23.600 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.040 * |
Rmerge | 0.097 * |
Total number of observations | 367482 * |
Number of reflections | 73906 |
Completeness [%] | 93.3 |
Redundancy | 4.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 9.5 * | Chen, L. C., (1992) Protein Eng., 5, 605. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 20 (%(w/v)) | ||
2 | 1 | drop | Tris | 100 (mM) | |
3 | 1 | drop | 10 (mM) | ||
4 | 1 | drop | 0.01 (mM) | ||
5 | 1 | drop | protain | 30 (mg/ml) | |
6 | 1 | reservoir | 31.6 (%(w/v)) | ||
7 | 1 | reservoir | Tris | 100 (mM) | |
8 | 1 | reservoir | 10 (mM) |