1YIB

Crystal Structure of the Human EB1 C-terminal Dimerization Domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-08-04
Detector	ADSC QUANTUM 4
Wavelength(s)	1.12704
Spacegroup name	C 2 2 21
Unit cell lengths	33.153, 108.332, 37.097
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.700 - 1.800
R-factor	0.224
Rwork	0.221
R-free	0.25900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.800
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.700	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.024	0.119
Number of reflections	11490
<I/σ(I)>	45	11.2
Completeness [%]	100.0	87.1
Redundancy	7	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	293	protein stock = EB1 C-terminal domain @ 15 mg/ml, MACF2 (1595-1637) peptide @ 8 mg/ml, well = 22% PEG 200 (v/v), 100 mM ammonium acetate pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K