6GE7

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	100
Detector technology	CCD
Collection date	2000-07-27
Detector	MAR CCD 165 mm
Wavelength(s)	1.2
Spacegroup name	P 32 2 1
Unit cell lengths	53.999, 53.999, 111.929
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	24.330 - 2.300
R-factor	0.19456
Rwork	0.192
R-free	0.24778
RMSD bond length	0.011
RMSD bond angle	1.534
Data reduction software	DENZO
Data scaling software	SORTRF
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0222)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.340
High resolution limit [Å]	2.300	2.300
Number of reflections	8916	435
<I/σ(I)>	18.3
Completeness [%]	98.9
Redundancy	9.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	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