3BEJ

Structure of human FXR in complex with MFA-1 and co-activator peptide

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-28
Detector	ADSC QUANTUM 210
Wavelength(s)	0.98793, 0.97931, 0.97907, 0.96863
Spacegroup name	P 21 21 21
Unit cell lengths	41.642, 90.889, 129.651
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.650 - 1.900
R-factor	0.203
Rwork	0.200
R-free	0.25400
Structure solution method	MAD
RMSD bond length	0.011
RMSD bond angle	1.271
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.065	0.577
Number of reflections	41792
<I/σ(I)>	10.7
Completeness [%]	100.0	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	16-22% PEG3350, 0.1M Bis-Tris, 4 mM YCl(3), 0.2M Ammonium acetate, 1 mM DTT. Protein was carboxymethylated with iodoacetic acid, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K