1Y3A
Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2004-04-03 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0093144 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 72.943, 112.785, 109.490 |
Unit cell angles | 90.00, 93.75, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.255 |
Rwork | 0.240 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bof |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 61384 | |
<I/σ(I)> | 11.2 | |
Completeness [%] | 78.2 | 96 |
Redundancy | 3.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 277 | PEG 8000, sucrose, sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |