4EMB
Crystal structure of a phosphoglycerate mutase gpmA from Borrelia burgdorferi B31
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-21 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.320, 116.750, 84.410 |
| Unit cell angles | 90.00, 107.67, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.300 |
| R-factor | 0.1775 |
| Rwork | 0.176 |
| R-free | 0.20130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lnt |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.442 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.360 | |
| High resolution limit [Å] | 2.300 | 10.290 | 2.300 |
| Rmerge | 0.078 | 0.044 | 0.473 |
| Number of reflections | 63406 | 730 | 4697 |
| <I/σ(I)> | 18.97 | 40.64 | 4.78 |
| Completeness [%] | 99.9 | 97.9 | 99.9 |
| Redundancy | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | BobuA.01013.a.A1 selenomethionine-labeled PW26571 at 27.7 mg/mL against CSHT B6: 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, 20% PEG8000, cryoprotectant: 20% ethylene glycol, crystal tracking ID 232024b6, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
