1G39

WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	200
Detector technology	CCD
Collection date	2000-02-24
Detector	ADSC QUANTUM 4
Wavelength(s)	1.00
Spacegroup name	P 1 21 1
Unit cell lengths	40.610, 37.330, 41.160
Unit cell angles	90.00, 90.04, 90.00

Refinement procedure

Resolution	20.600 - 1.220
R-factor	0.2552
Rwork	0.256
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	peptide model with selenomethionine substituted at position 12 solved by MAD
RMSD bond length	0.013
RMSD bond angle	1.700
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.600	1.280
High resolution limit [Å]	1.220	1.220
Rmerge	0.051	0.497 *
Number of reflections	36802
<I/σ(I)>	24.6	2.2
Completeness [%]	99.8	100
Redundancy	5.3	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8.5	277	PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	peptide	10 (mg/ml)
2	1	reservoir	PEG4000	24 (%)
3	1	reservoir	Tris-HCl	80 (mM)
4	1	reservoir		0.16 (M)