1HQO

CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-02
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9791, 0.9789, 0.9686
Spacegroup name	P 21 21 21
Unit cell lengths	64.310, 69.190, 149.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.221 *
Rwork	0.221
R-free	0.27500
Structure solution method	MAD
RMSD bond length	0.012
RMSD bond angle	22.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.048	0.320
Total number of observations	168715 *
Number of reflections	29499 *
<I/σ(I)>	15.4
Completeness [%]	97.6	99.5
Redundancy	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8 *	293	NaCl, Bicine, Tris-HCl, alpha-chymotrypsin, pH 8.8, VAPOR DIFFUSION, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.25 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	drop		0.3 (M)
4	1	drop	alpha-chymotrypsin	0.01-0.001 (mg/ml)
5	1	reservoir		2.5-3.0 (M)
6	1	reservoir	Bicine	100 (mM)