1BH2
A326S MUTANT OF AN INHIBITORY ALPHA SUBUNIT
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1996-12 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 79.584, 79.584, 105.556 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 18.000 - 2.100 |
R-factor | 0.19 |
Rwork | 0.190 |
R-free | 0.25000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gia |
RMSD bond length | 0.009 |
RMSD bond angle | 22.508 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 20438 | |
<I/σ(I)> | 10.8 | 4.6 |
Completeness [%] | 88.4 | 88.1 |
Redundancy | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6 | 21 * | Coleman, D.E., (1994) Science, 265, 1405. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25-30 (mg/ml) | |
2 | 1 | drop | 0.3 (mM) | ||
3 | 1 | drop | 5 (mM) | ||
4 | 1 | drop | 5 (mM) | ||
5 | 1 | drop | DTT | 10 (mM) | |
6 | 1 | drop | sodium acetate | 200 (mM) | |
7 | 1 | reservoir | ammonium sulfate | 1.8-1.9 (M) |