1MYR
MYROSINASE FROM SINAPIS ALBA
Experimental procedure
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-09 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 134.300, 136.400, 80.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.400 - 1.640 |
R-factor | 0.152 |
Rwork | 0.152 |
R-free | 0.18700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cbg |
RMSD bond length | 0.022 |
RMSD bond angle | 23.800 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.400 | 1.730 |
High resolution limit [Å] | 1.640 | 1.640 |
Rmerge | 0.065 | 0.190 |
Number of reflections | 88638 | |
<I/σ(I)> | 7.7 | 2.4 |
Completeness [%] | 98.3 | 90.7 |
Redundancy | 4.6 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | HANGING DROP METHOD, 12 MG/ML PROTEIN IN 30 MM HEPES, PH 6.5, 0.05 % NAN3 PRECIPITANT 66 % SAT. AMMONIUM SULFATE, 100MM TRIS-HCL, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | myrosinase | 12 (mg/ml) | |
2 | 1 | drop | HEPES | 30 (mM) | |
3 | 1 | drop | 0.05 (%) | ||
4 | 1 | reservoir | ammonium sulfate | 66 (%sat) | |
5 | 1 | reservoir | Tris-HCl | 100 (mM) |