2BRR
Complex of the neisserial PorA P1.4 epitope peptide and two Fab- fragments (antibody MN20B9.34)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-05-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.666, 63.833, 124.701 |
| Unit cell angles | 90.00, 86.58, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.950 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ce1 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.408 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.080 | 0.390 |
| Number of reflections | 60806 | |
| <I/σ(I)> | 14.3 | 3.1 |
| Completeness [%] | 96.0 | 92.1 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | 0.2 M AMMONIUM SULPHATE, 0.1 M SODIUM ACETATE/ACETIC ACID (PH 4.0) AND 25% W/V PEG 3000 |
