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