2XNX
BC1 fragment of streptococcal M1 protein in complex with human fibrinogen
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-10 |
| Detector | MARRESEARCH MX-300 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 112.723, 216.866, 140.807 |
| Unit cell angles | 90.00, 102.54, 90.00 |
Refinement procedure
| Resolution | 116.250 - 3.300 |
| R-factor | 0.279 |
| Rwork | 0.277 |
| R-free | 0.32500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3e1i |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.153 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 116.250 | 3.480 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.110 | 0.500 |
| Number of reflections | 90704 | |
| <I/σ(I)> | 5.8 | 1.4 |
| Completeness [%] | 96.7 | 91.5 |
| Redundancy | 2.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 16% PEG 3350, 0.2 M SODIUM TARTRATE WITH SEEDS GROWN IN 0.6 M K2/NA2 PO4, 0.12 M (NH4)2SO4, 0.1 M HEPES, PH 7.5 |
