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 |