1J78

Crystallographic analysis of the human vitamin D binding 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	IMAGE PLATE
Collection date	1999-04-17
Detector	MARRESEARCH
Wavelength(s)	0.9116
Spacegroup name	P 43
Unit cell lengths	132.248, 132.248, 73.179
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.380 - 2.310
R-factor	0.2201 *
Rwork	0.220
R-free	0.25180 *
Structure solution method	COMBINED MAD AND MIRAS
RMSD bond length	0.006
RMSD bond angle	1.170 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.350
High resolution limit [Å]	2.310	2.310
Rmerge	0.031	0.209
Total number of observations	187531 *
Number of reflections	55444
<I/σ(I)>	22.7	5.2
Completeness [%]	99.2	99.6
Redundancy	3.4	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6	293	Verboven, C.C., (1995) J. Steroid Biochem. Mol. Biol., 54, 11. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	7.5 (%(v/v))
2	1	reservoir	acetate	0.1 (M)	pH4.6
3	1	drop	protein	30 (mg/ml)