3GH1
Crystal structure of predicted nucleotide-binding protein from Vibrio cholerae
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-03-27 |
Detector | MAR scanner 180 mm plate |
Wavelength(s) | 0.9791 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.034, 181.546, 95.772 |
Unit cell angles | 90.00, 103.32, 90.00 |
Refinement procedure
Resolution | 19.920 - 1.900 |
R-factor | 0.172 |
Rwork | 0.169 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pmb |
RMSD bond length | 0.023 |
RMSD bond angle | 1.919 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.2.5) |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 27.096 |
High resolution limit [Å] | 1.832 |
Rmerge | 0.159 |
Number of reflections | 149929 |
<I/σ(I)> | 2.955 |
Completeness [%] | 88.0 |
Redundancy | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 0.15M Malic acid, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |