3TMG
Crystal structure of Glycine betaine, L-proline ABC transporter, glycine/betaine/L-proline-binding protein (ProX) from Borrelia burgdorferi
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-07 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.978560 |
| Spacegroup name | P 1 |
| Unit cell lengths | 52.400, 56.750, 107.060 |
| Unit cell angles | 92.30, 102.40, 105.25 |
Refinement procedure
| Resolution | 49.160 - 1.900 |
| R-factor | 0.177 |
| Rwork | 0.175 |
| R-free | 0.21400 |
| Structure solution method | MR |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.569 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.160 | 8.500 | 1.950 |
| High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
| Rmerge | 0.086 | 0.034 | 0.447 |
| Number of reflections | 88358 | 1840 | 6512 |
| <I/σ(I)> | 17.74 | 39.5 | 3.6 |
| Completeness [%] | 96.9 | 98.7 | 95.7 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 290 | EBS internal tracking number 220361B9.PACT B9: 0.2 M LiCl, 0.1 M MES pH 6, 20% PEG 6000. BobuA.17327.a.A2 PW31644 at 26 mg/mL, vapor diffusion, sitting drop, temperature 290K, VAPOR DIFFUSION, SITTING DROP |
