2HFF
Crystal structure of CB2 Fab
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-06-12 |
| Detector | CUSTOM-MADE |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.710, 72.985, 89.919 |
| Unit cell angles | 109.42, 100.96, 96.10 |
Refinement procedure
| Resolution | 30.000 - 1.950 |
| R-factor | 0.19229 |
| Rwork | 0.189 |
| R-free | 0.22079 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | chains A B from pdb 2HG9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.192 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Number of reflections | 63805 | |
| <I/σ(I)> | 6.9 | 1.8 |
| Completeness [%] | 98.0 | 91.8 |
| Redundancy | 3.4 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Crystals were grown in hanging drops with 1:1 ratio of protein to well solution consisting of 100 mM Hepes, pH 7.5, 20% PEG 10K, and then frozen in mother liquor with 25% PEG 400 |
