1BG9
BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 288 |
Detector technology | AREA DETECTOR |
Collection date | 1992-04 |
Detector | SIEMENS |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 135.200, 135.200, 79.600 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.800 |
R-factor | 0.151 |
Rwork | 0.151 |
R-free | 0.24900 |
Structure solution method | REFINEMENT DIFFERENCE FOURIER |
Starting model (for MR) | 1amy |
RMSD bond length | 0.015 * |
RMSD bond angle | 23.600 * |
Data reduction software | XENGEN ((HOWARD) |
Data scaling software | XENGEN |
Phasing software | X-PLOR (2.1) |
Refinement software | X-PLOR (2.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.900 | |
High resolution limit [Å] | 2.729 | 2.729 |
Rmerge | 0.092 | 0.270 |
Total number of observations | 61039 * | |
Number of reflections | 17688 | |
<I/σ(I)> | 16.6 | 1.7 |
Completeness [%] | 90.5 | 44.8 |
Redundancy | 2.9 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.7 | Svensson, B., (1987) J. Biol. Chem., 262, 13682. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 1 (mM) | ||
2 | 1 | drop | MES | 10 (mM) | |
3 | 1 | drop | protein | 4-16 (mg/ml) | |
4 | 1 | reservoir | ammonium sulfate | 10 (%sat) |