1BGA
BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA
Experimental procedure
Source type | SYNCHROTRON |
Source details | LURE |
Synchrotron site | LURE |
Temperature [K] | 176 |
Detector technology | IMAGE PLATE |
Collection date | 1996-10 |
Detector | MARRESEARCH |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 205.460, 205.460, 155.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.400 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cbg |
RMSD bond length | 0.009 |
RMSD bond angle | 24.000 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | X-PLOR (3.843) |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.540 | 2.460 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.083 * | 0.300 |
Total number of observations | 584536 * | |
Number of reflections | 117344 | |
<I/σ(I)> | 8.3 | 1.8 |
Completeness [%] | 97.3 | 92.3 |
Redundancy | 4.7 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | co-crystallization * | 8.3 | PROTEIN WAS CRYSTALLIZED FROM 1.3 M NA/K PHOSPHATE, PH 8.3, 5 MICRO-L PROTEIN, 14 MG/ML, 5 MICRO-L RESERVOIR |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | phosphate | 1.3 (M) | |
2 | 1 | drop | inhibitor |