5V0V

Crystal structure of Equine Serum Albumin complex with etodolac

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-04-17
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97949
Spacegroup name	P 61
Unit cell lengths	94.209, 94.209, 141.819
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.450
R-factor	0.1833
Rwork	0.180
R-free	0.23780
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5bqf
RMSD bond length	0.007
RMSD bond angle	1.144
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.490
High resolution limit [Å]	2.450	6.650	2.450
Rmerge	0.088	0.057	0.574
Rmeas	0.102	0.065	0.673
Rpim	0.050	0.032	0.343
Number of reflections	26311		1304
<I/σ(I)>	4.8		1.2
Completeness [%]	99.9	99.9	98.6
Redundancy	4	3.9	3.5
CC(1/2)		0.993	0.753

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	289	1 ul of 34 mg/ml protein in 10 mM Tris pH 7.5 and 150 mM NaCl buffer was mixed with 1 ul of the well condition (0.2 M Li2SO4, 0.1 M Tris:HCl, 2.0 M (NH4)2SO4 final pH 7.4) and equilibrated against well solution in 15 Well Crystallization Plate (Qiagen). Crystals were soaked with 10 mM Etodolac.