6GHH

Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SEALED TUBE
Source details	OXFORD DIFFRACTION NOVA
Temperature [K]	100
Detector technology	CCD
Collection date	2016-05-19
Detector	AGILENT ATLAS CCD
Wavelength(s)	1.54
Spacegroup name	P 32 2 1
Unit cell lengths	53.588, 53.588, 111.607
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	13.800 - 1.900
R-factor	0.1992
Rwork	0.197
R-free	0.24751
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gx9
RMSD bond length	0.010
RMSD bond angle	1.697
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0222)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	13.800	2.010
High resolution limit [Å]	1.900	1.900
Number of reflections	17826
<I/σ(I)>	8.2
Completeness [%]	99.7
Redundancy	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3	293.2	protein 20 mg/mL, ligand 10mM, 20mM Tris buffer, pH 8, which were mixed with 4 microliter of well solution. Drops were equilibrated against 1 mL of well solution containing 1.43 M sodium citrate and 0.1M Hepes, pH 7.5