3MMT
Crystal structure of fructose bisphosphate aldolase from Bartonella henselae, bound to fructose bisphosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-02 |
| Detector | ADSC QUANTUM Q315 |
| Wavelength(s) | 0.97740 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.390, 127.710, 157.630 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.890 - 2.350 |
| R-factor | 0.179 |
| Rwork | 0.177 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3kx6 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.180 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.890 | 2.410 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.099 | 0.553 |
| Number of reflections | 61670 | |
| <I/σ(I)> | 4.2 | |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 8.9 | 8.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | 0.2 M NAOAC, 0.1 M TRIS PH 8.5, 30% PEG 4000, protein AT 21 MG/ML, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
