1QG5
HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORM A)
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 | 1997-09-15 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 55.470, 82.110, 66.760 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 9.500 - 2.000 |
Rwork | 0.192 |
R-free | 0.28300 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 * |
RMSD bond angle | 2.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 12.900 * | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.066 * | 0.460 * |
Number of reflections | 9631 | |
<I/σ(I)> | 12.7 | |
Completeness [%] | 90.9 | 91.2 |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | THE CRYSTAL WAS GROWN AT PH 7.9, HANGING DROP METHOD. DROP CONTAINED 2.5M (NH4) 2SO4, 180MM TRIZMA BUFFER, AND 20MG/ML PROTEIN REMARK 290, 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) |