1NR0

Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Collection date	2002-09-12
Detector	ADSC QUANTUM 4
Wavelength(s)	0.98
Spacegroup name	P 1 21 1
Unit cell lengths	64.845, 65.174, 69.240
Unit cell angles	90.00, 98.28, 90.00

Refinement procedure

Resolution	23.600 * - 1.700
R-factor	0.199
Rwork	0.199
R-free	0.23000
Structure solution method	SIRAS
RMSD bond length	0.009
RMSD bond angle	27.100 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHELXD
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.600 *	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.045	0.273
Number of reflections	61821
Completeness [%]	98.6	97.7
Redundancy	4.02

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	316	PEG 8000, Mn chloride, cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 316K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3-4 (mg/ml)
2	1	reservoir	MES	0.1 (M)
3	1	reservoir	PEG8000	20 (%)
4	1	reservoir		10 (mM)
5	1	reservoir	glycerol	3 (%)	pH6.0