6YG9

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN (HSA) IN COMPLEX WITH GN-07.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06DA
Synchrotron site	SLS
Beamline	X06DA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-08-04
Detector	DECTRIS PILATUS3 X 1M
Wavelength(s)	1.000000
Spacegroup name	C 1 2 1
Unit cell lengths	197.722, 38.141, 95.372
Unit cell angles	90.00, 105.88, 90.00

Refinement procedure

Resolution	58.510 - 1.890
R-factor	0.243
Rwork	0.239
R-free	0.31300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	in-house structure
RMSD bond length	0.010
RMSD bond angle	1.200
Data reduction software	XDS
Data scaling software	Aimless (0.5.21)
Phasing software	PHASER
Refinement software	BUSTER

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	58.510	1.897
High resolution limit [Å]	1.890	1.890
Rmeas	0.077	0.620
Rpim	0.043	0.344
Total number of observations	156458	20574
Number of reflections	53533	7654
<I/σ(I)>	11.7	2.3
Completeness [%]	96.3	91.9
Redundancy	2.9	2.7
CC(1/2)	0.996	0.735

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	Essentially defatted human serum albumin from Sigma was purified by size exclusion chromatography to obtain pure monomeric protein. The purified HSA was dissolved in 20 mM potassium phosphate (pH 7.0) and concentrated to 120 mg/mL. To the HSA solution we added 10 mM cpdX and 3 mM myristate, dissolved DMSO. The final concentration of DMSO was 5% (v/v). The crystal was grown by the hanging drop vapor diffusion method using a reservoir solution containing 50 mM sodium-potassium-phosphate (pH 7.0), and 30% polyethylene glycol 3350. For crystallization 1 uL of HSA/cpdX solution was equilibrated against 1 uL of reservoir solution. After about one-week, colorless crystals appeared.