1CM9

CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	123
Detector technology	IMAGE PLATE
Collection date	1998-08
Detector	RIGAKU RAXIS IV
Wavelength(s)	0.9793, 0.9790, 0.9871
Spacegroup name	C 1 2 1
Unit cell lengths	70.250, 57.610, 49.560
Unit cell angles	90.00, 130.85, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.24
Rwork	0.240
R-free	0.27500
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.311
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000
High resolution limit [Å]	2.100	2.100 *
Rmerge	0.083 *	0.381 *
Number of reflections	8259
Completeness [%]	92.8
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.6		used seeding, Fernandez, E,J., (2000) J.Appl.Crystallogr., 33, 168. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	PEG4000	11 (%)
3	1	reservoir	2-propanol	11 (%)
4	1	reservoir	sodium citrate	0.1 (M)