5IIU

Crystal structure of Equine Serum Albumin in the presence of 10 mM zinc at pH 6.9

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2014-12-04
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.979
Spacegroup name	P 61
Unit cell lengths	93.746, 93.746, 141.789
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	80.010 - 2.300
R-factor	0.1817
Rwork	0.179
R-free	0.23950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5iih
RMSD bond length	0.008
RMSD bond angle	1.247
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	80.010	80.000	2.340
High resolution limit [Å]	2.300	6.240	2.300
Rmerge	0.078	0.028
Number of reflections	31099
<I/σ(I)>	7.6
Completeness [%]	99.3	98.4	99
Redundancy	9.7	9.3	9.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.9	289	1 ul of 30 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, 5 mM ZnCl2, final pH 6.9) and equilibrated against well solution in 15 Well Crystallization Plate (Qiagen). Crystals were soaked with 50 mM ZnCl2 in 100 mM Tris, final pH 6.9, to final concentration of 10 mM