1QJU

HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	277
Detector technology	FILM
Collection date	1994-04-15
Detector	KODAK FILM
Spacegroup name	P 2 21 21
Unit cell lengths	362.600, 347.100, 334.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.800
R-factor	0.206
Rwork	0.206
R-free	0.21200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1aym
RMSD bond length	0.006
RMSD bond angle	26.700 *
Data reduction software	PURDUE (DATA PROCESSING PACKAGE)
Data scaling software	PURDUE (DATA PROCESSING PACKAGE)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.930
High resolution limit [Å]	2.800	2.800
Rmerge	0.078	0.123 *
Number of reflections	590371
Completeness [%]	58.7	44.5 *
Redundancy	1.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8-10 (mg/ml)
2	1	drop	HEPES	0.25 (mM)
3	1	drop	PEG8000	0.5-1.5 (%)
4	1	reservoir	PEG8000	0.5-1.5 (%)