3MD7
Crystal structure of a beta-lactamase-like protein bound to GMP from brucella melitensis
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 | 2010-03-08 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9774 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 72.890, 75.250, 98.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.850 - 1.270 |
| R-factor | 0.108 |
| Rwork | 0.107 |
| R-free | 0.13400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | structure solved by molecular replacement using initial model from iodide SAD phasing can also be solved using anomalous signal from Mn and K |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.873 |
| 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] | 50.000 | 1.300 |
| High resolution limit [Å] | 1.270 | 1.270 |
| Rmerge | 0.051 | 0.489 |
| Number of reflections | 71257 | |
| <I/σ(I)> | 28.3 | 3.9 |
| Completeness [%] | 99.7 | 97.2 |
| Redundancy | 9.5 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 290 | MD PACT SCREEN, H9: 20% PEG 3350, 200MM K/NA TARTRATE, 100MM BISTRISPROPANE PH 8.6; BRABA.11339.A AT 19.6MG/ML, PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |
