1BH5
HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-03-23 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 41 |
Unit cell lengths | 67.280, 67.280, 164.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.200 |
R-factor | 0.25 * |
Rwork | 0.180 |
R-free | 0.28000 * |
Structure solution method | MR |
Starting model (for MR) | 1fro |
RMSD bond length | 0.010 |
RMSD bond angle | 0.030 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.048 | 0.128 |
Number of reflections | 33195 | |
<I/σ(I)> | 27 | 5.5 |
Completeness [%] | 89.7 | 63 * |
Redundancy | 3.5 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.8 | 15 * | Cameron, A.D., (1997) EMBO J., 16, 3386. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG2000 | 12.5-15 (%(w/v)) | |
2 | 1 | drop | MES | 25 (mM) | |
3 | 1 | drop | 0.05 (M) | ||
4 | 1 | drop | protein | 6 (mg/ml) | |
5 | 1 | drop | 2-mercaptoethanol | 0.5 (%) | |
6 | 1 | drop | S-benzyl-glutathione | 1 (mM) | |
7 | 1 | reservoir | PEG2000 | 25-30 (%(w/v)) | |
8 | 1 | reservoir | MES | 50 (mM) | |
9 | 1 | reservoir | 0.1 (M) |