1OVN

Crystal Structure and Functional Analysis of Drosophila Wind-- a PDI-Related Protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, Hamburg
Beamline	X11
Temperature [K]	100
Detector technology	CCD
Collection date	2002-07-31
Detector	MARRESEARCH
Wavelength(s)	0.811
Spacegroup name	C 1 2 1
Unit cell lengths	106.678, 50.358, 98.616
Unit cell angles	90.00, 112.84, 90.00

Refinement procedure

Resolution	37.640 * - 1.900
R-factor	0.2179
Rwork	0.216
R-free	0.25570 *
Structure solution method	SIRAS
Starting model (for MR)	NONE
RMSD bond length	0.023
RMSD bond angle	2.130 *
Data reduction software	XPREP
Data scaling software	SCALEPACK
Phasing software	SHELXD
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.640	2.000
High resolution limit [Å]	1.900	1.900
Rmerge		0.196 *
Number of reflections	38218
<I/σ(I)>	13.96	4.77
Completeness [%]	0.0 *	99.6
Redundancy	4.5	3.79

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	20 *	mixing 6ul [5.8mg/ml Wind in 5mM HEPES pH7.5, 25mM NaCl, 0.0025%(V/V) beta-mercaptoethanol] with 3ul [0.1M MES pH6.1, 0.1M CsCl, 2mM CaCl2, 16%(V/V) PEG 300] cryo-condition: 0.1M Mes pH6.1, 20%(V/V) PEG 300, 10%(V/V)glycerol, 0.1M CsCl, 2mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.8 (mg/ml)
2	1	drop	HEPES	5 (mM)	pH7.5
3	1	drop		25 (mM)
4	1	drop	beta-mercaptoethanol	0.0025 (%(v/v))
5	1	reservoir	MES	0.1 (M)	pH6.1
6	1	reservoir		0.1 (M)
7	1	reservoir		2 (mM)
8	1	reservoir	PEG300	16 (%(v/v))