1C1Z

CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-05-25
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	159.500, 164.800, 114.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.870
R-factor	0.238
Rwork	0.238
R-free	0.24400
Structure solution method	MIR-MAD COMBINATION
RMSD bond length	0.009
RMSD bond angle	24.570 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	SHARP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.050
High resolution limit [Å]	2.870	2.870
Rmerge	0.086	0.430
Total number of observations	103699 *
Number of reflections	32406
Completeness [%]	93.2	60.1
Redundancy	3.2	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.2	277	Saxena, A., (1998) Acta Crystallogr., Sect.D, 54, 1450. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium sulfate	1.6-2.0 (M)
3	1	reservoir	sodium carbonate	0.2 (%)