4FRV

Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the American Quarter Horse

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2010-08-12
Detector	NOIR-1
Wavelength(s)	0.827
Spacegroup name	C 1 2 1
Unit cell lengths	64.790, 44.160, 60.110
Unit cell angles	90.00, 95.45, 90.00

Refinement procedure

Resolution	16.286 - 1.100
R-factor	0.1204
Rwork	0.119
R-free	0.13800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cyn
RMSD bond length	0.007
RMSD bond angle	1.286
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	PHENIX ((phenix.refine: 1.8_1069))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	16.290	1.160
High resolution limit [Å]	1.100	1.100
Rmerge	0.052	0.242
Number of reflections	61849
<I/σ(I)>	12.4	4.2
Completeness [%]	90.2	53.4
Redundancy	3.3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2		0.1M MES, 10mM ZnCl2, 10% glycerol, 28% PEG MME 550, pH 7.2, VAPOR DIFFUSION, HANGING DROP