4CGT
DELETION MUTANT DELTA(145-150), F151D OF CYCLODEXTRIN GLYCOSYLTRANSFERASE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1994-09 |
Detector | SIEMENS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 94.500, 104.600, 113.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.600 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.27200 |
Structure solution method | X-PLOR |
Starting model (for MR) | WILD-TYPE WITH RESIDUES 145 - 151 DELETED |
RMSD bond length | 0.012 |
RMSD bond angle | 25.700 * |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 26.630 |
High resolution limit [Å] | 2.600 |
Number of reflections | 30720 |
Completeness [%] | 88.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.7 * | Hofmann, B.E., (1989) J.Mol.Biol., 209, 793. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein solution | 50 (%(v/v)) | |
2 | 1 | drop | CGTase | 7-15 (mg/ml) | |
3 | 1 | drop | Tris-HCl | 50 (mM) | |
4 | 1 | drop | PEG1500 | 0.5 (%) | |
5 | 1 | reservoir | ammonium sulphate | 0.9-1.0 (M) | |
6 | 1 | reservoir | CGTase | 7-15 (mg/ml) | |
7 | 1 | reservoir | Tris-HCl | 50 (mM) | |
8 | 1 | reservoir | PEG1500 | 0.5 (%) |