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 |
