1B8E
HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE D03B-MX1 |
Synchrotron site | LNLS |
Beamline | D03B-MX1 |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Collection date | 1997-09 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 55.640, 81.650, 66.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 9.500 - 1.950 |
Rwork | 0.189 |
R-free | 0.25600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | B-LG LATTICE Y FROM MIXTURE OF GENETIC VARIANTS A AND B |
RMSD bond length | 0.009 * |
RMSD bond angle | 2.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 * | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.085 * | 0.440 * |
Number of reflections | 9834 | |
<I/σ(I)> | 9.2 | |
Completeness [%] | 86.4 | 88.8 |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | METHOD IN PRESENCE OF AMMONIUM SULPHATE 2.5 M, 180MM TRIZMA BUFFER AT A PROTEIN CONCENTRATION OF 20MG/ML, pH 7.9, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2.5 (M) | |
3 | 1 | reservoir | Tris-HCl | 180 (mM) |