1PGU

YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-01-02
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97902,0.918,0.97932
Spacegroup name	P 1 21 1
Unit cell lengths	60.800, 154.530, 69.000
Unit cell angles	90.00, 90.65, 90.00

Refinement procedure

Resolution	25.000 * - 2.300
R-factor	0.202
Rwork	0.202
R-free	0.25700
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	26.700 *
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]	25.000	2.440
High resolution limit [Å]	2.300	2.300
Rmerge	0.069 *	0.230 *
Total number of observations	192792 *
Number of reflections	51350 *
Completeness [%]	90.9 *	93.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	15% PEG 4000, 100mM NaCl, 100mM Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	HEPES	100 (mM)	pH7.5
3	1	reservoir		200 (mM)
4	1	reservoir	PEG4000	13 (%(w/v))