1ELZ
E. COLI ALKALINE PHOSPHATASE MUTANT (S102G)
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 292 |
| Detector technology | AREA DETECTOR |
| Collection date | 1996-07 |
| Detector | SIEMENS-NICOLET X100 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 164.570, 164.500, 138.590 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9.000 - 2.800 |
| R-factor | 0.138 |
| Rwork | 0.138 |
| R-free | 0.17300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1alk |
| RMSD bond length | 0.015 |
| RMSD bond angle | 24.300 * |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.130 | 0.372 |
| Number of reflections | 26363 | |
| <I/σ(I)> | 5.3 | 1.4 |
| Completeness [%] | 96.0 | 85 |
| Redundancy | 3.5 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9.5 * | 25 MG/ML PROTEIN IN 39% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 30 (mg/ml) | |
| 2 | 1 | drop | ammonium sulfate | 20 (%sat) | |
| 3 | 1 | drop | Tris-HCl | 100 (mM) | |
| 4 | 1 | drop | 10 (mM) | ||
| 5 | 1 | drop | 100 (mM) | ||
| 6 | 1 | reservoir | ammonium sulfate | 36-39 (%sat) |
