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 |
