6UKO

Structure analysis of full-length mouse bcs1 complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2013-04-23
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	C 1 2 1
Unit cell lengths	254.055, 161.127, 132.595
Unit cell angles	90.00, 107.27, 90.00

Refinement procedure

Resolution	24.910 - 4.400
R-factor	0.3584
Rwork	0.357
R-free	0.40670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	cryoEM
RMSD bond length	0.004
RMSD bond angle	0.798
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	PHENIX (1.17_3644)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	4.560
High resolution limit [Å]	4.400	4.400
Rmerge	0.078
Rpim	0.034
Number of reflections	32257	3169
<I/σ(I)>	19.09	1.38
Completeness [%]	99.9	100
Redundancy	6.2	5.6
CC(1/2)		0.306

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	277	Protein was premixed with 2mM ATP-gamma-S and 20 mM MgCl2 incubated for 30 min on ice, then centrifuged and the supernatant was mixed with 100 mM Tris pH 9.0, 100 mM NaCl, 60 mM MgCl2, 15% PEG400