1AJX

HIV-1 PROTEASE IN COMPLEX WITH THE CYCLIC UREA INHIBITOR AHA001

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	1996-04
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	59.000, 86.800, 46.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.000
R-factor	0.161
Rwork	0.161
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ajv
RMSD bond length	0.025
RMSD bond angle	26.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.050	0.178
Total number of observations	62019 *
Number of reflections	14634
Completeness [%]	84.3	48

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	5.5	4 *	CRYSTALLIZATION WAS PERFORMED BY VAPOR DIFFUSION. PROTEASE (2 MG/ML) AND INHIBITOR (40 MM IN DMSO) WAS MIXED IN A RATIO OF 1:1 AND SUBJECTED TO COCRYSTALLIZATION. DROPS CONSISTING OF 5 MICROLITERS OF THE PROTEASE-INHIBITOR MIXTURE PLUS 5 MICROLITERS OF THE CRYSTALLIZATION BUFFER (50 MM MES PH 5.5, 0.4 M NACL AND 0.02% (W/V) NAN3) WERE EQUILIBRATED AGAINST THE SAME BUFFER AT 4 DEGREES C., vapor diffusion, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protease	2 (mg/ml)
2	1	drop	inhibitor	40 (mM)	in DMSO
3	1	drop	MES	50 (mM)
4	1	drop		0.4 (M)
5	1	drop		0.02 (%(w/v))
6	1	reservoir	MES	50 (mM)
7	1	reservoir		0.4 (M)
8	1	reservoir		0.02 (%(w/v))