6MDQ
Crystal structure of equine serum albumin in complex with testosterone
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-07-06 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 61 |
Unit cell lengths | 94.244, 94.244, 142.345 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.150 |
R-factor | 0.1853 |
Rwork | 0.183 |
R-free | 0.22550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3v08 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.821 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.190 |
High resolution limit [Å] | 2.150 | 5.830 | 2.150 |
Rmerge | 0.071 | 0.034 | 1.027 |
Rmeas | 0.076 | 0.037 | 1.112 |
Rpim | 0.028 | 0.014 | 0.424 |
Total number of observations | 298193 | ||
Number of reflections | 39149 | 1923 | 1910 |
<I/σ(I)> | 10 | ||
Completeness [%] | 99.7 | 95.3 | 100 |
Redundancy | 7.6 | 7.2 | 6.8 |
CC(1/2) | 0.999 | 0.811 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.2 ul of 15 mg/ml protein was mixed with 0.2 ul of the well condition (1.8 M ammonium dihydrogen citrate, pH 7.0) and equilibrated against well solution in 96-Well sitting drop crystallization plate (Swissci). Testosterone powder was added to the crystallization drop |