1LXD
CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-11-10 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 105.282, 30.714, 51.326 |
Unit cell angles | 90.00, 94.57, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.400 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.29800 |
Structure solution method | MAD |
RMSD bond length | 0.014 |
RMSD bond angle | 2.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MADSYS |
Refinement software | X-PLOR (3.85) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.480 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.090 * | |
Number of reflections | 6485 | |
<I/σ(I)> | 16.7 | 5.92 |
Completeness [%] | 99.3 | 99.5 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 8000, 0.1 M TRIS PH 8.5, AND 0.2 M CALCIUM ACETATE. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
10 | 1 | reservoir | PEG8000 | 20 (%) | |
2 | 1 | drop | dithiothreitol | 0.5 (mM) | |
3 | 1 | drop | PMSF | 0.5 (mM) | |
4 | 1 | drop | EDTA | 0.5 (mM) | |
5 | 1 | drop | calcium acetate | 0.1 (M) | |
6 | 1 | drop | Tris-HCl | 0.05 (mM) | |
7 | 1 | drop | PEG8000 | 10 (%) | |
8 | 1 | reservoir | calcium acetate | 0.2 (M) | |
9 | 1 | reservoir | Tris-HCl | 0.1 (M) |