6CI6

Crystal structure of equine serum albumin in complex with nabumetone

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	93.879, 93.879, 140.787
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.010 - 2.800
R-factor	0.1858
Rwork	0.182
R-free	0.25570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3v08
RMSD bond length	0.007
RMSD bond angle	1.088
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]	50.010	50.000	2.850
High resolution limit [Å]	2.800	7.590	2.800
Rmerge	0.115	0.065	0.660
Rmeas	0.129	0.073	0.742
Rpim	0.057	0.032	0.335
Number of reflections	17321	904	871
<I/σ(I)>	4.6
Completeness [%]	100.0	99.9	100
Redundancy	5.1	5	4.9
CC(1/2)		0.995	0.816

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 7.4 and 150 mM NaCl buffer was mixed with 1 ul of the well condition (0.2 M Li2SO4, 0.1 M Tris:HCl, 2.2 M (NH4)2SO4 final pH 7.4) and equilibrated against well solution in 15 Well Crystallization Plate (Qiagen). Crystals were soaked with 10 mM nabumetone