2GPR
GLUCOSE PERMEASE IIA FROM MYCOPLASMA CAPRICOLUM
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1995-11 |
Detector | SIEMENS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.330, 47.650, 71.890 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.186 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gpr |
RMSD bond length | 0.018 |
RMSD bond angle | 20.200 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | AMoRE |
Refinement software | TNT (5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.500 | 2.500 * |
Rmerge | 0.063 * | 0.162 * |
Total number of observations | 12034 * | |
Number of reflections | 4952 | |
<I/σ(I)> | 28.3 | |
Completeness [%] | 97.0 | 85.3 * |
Redundancy | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 20-30% PEG 3000, 0.3MM ZNCL2, 100MM TRIS-HCL BUFFER, PH 7.5. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3000 | 20-26 (%) | |
2 | 1 | reservoir | 0.3 (mM) | ||
3 | 1 | reservoir | Tris-HCl | 100 (mM) | |
4 | 1 | drop | protein | 10 (mg/ml) | |
5 | 1 | drop | Tris-HCl | 10 (mM) |