2HFG
Crystal structure of hBR3 bound to CB3s-Fab
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 | 2004-12-17 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | I 21 3 |
Unit cell lengths | 146.408, 146.408, 146.408 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.610 |
R-factor | 0.20052 |
Rwork | 0.195 |
R-free | 0.25245 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | CB2-Fab |
RMSD bond length | 0.010 |
RMSD bond angle | 1.256 |
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 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 16168 | |
<I/σ(I)> | 11.7 | 3.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Drops contained 2.1 microliters protein solution (pH 6.5) and 2.9 microliters of (0.1M citric acid pH 3.0, 24% PEG 3350, and 0.1 M Praseodymium (III) acetate) over a reservoir of 24% PEG 3350. pH of final drop ~4.5. |