1AUM

HIV CAPSID C-TERMINAL DOMAIN (CAC146)

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	100
Detector technology	CCD
Collection date	1997-07
Spacegroup name	I 41
Unit cell lengths	60.480, 60.480, 59.690
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 3.000
R-factor	0.355
Rwork	0.355
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	C-TERMINAL CAPSID (151 - 231)
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.044 *	0.368 *
Number of reflections	2681
<I/σ(I)>	18	2.5
Completeness [%]	99.1	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8	4 *	CRYSTALS OF CAC(146-231) WERE GROWN AT 4C IN 8 MICROLITER SITTING DROPS CONTAINING A 1:1 MIXTURE OF PROTEIN SOLUTION (2.1 MM CA(151-231) IN 10 MM TRIS (PH 8.0) AND 2 MM 2-MERCAPTOETHANOL) AND RESERVOIR SOLUTION (2.0 M AMMONIUM SULFATE), vapor diffusion - sitting drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	0.105 (mg/ml)
2	1	drop	Tris-HCl	5 (mM)
3	1	drop	2-mercaptoethanol	1 (mM)
4	1	drop	ammonium sulfate	1 (M)
5	1	reservoir	ammonium sulfate	2 (M)