2AQU

Structure of HIV-1 protease bound to atazanavir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	2005-07-18
Detector	ADSC QUANTUM 315
Wavelength(s)	1.1
Spacegroup name	P 61
Unit cell lengths	62.411, 62.411, 82.569
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.830 - 2.000
R-factor	0.227
Rwork	0.227
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1sgu
RMSD bond length	0.021
RMSD bond angle	2.300
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge		0.472
Number of reflections	12320
<I/σ(I)>		2.5
Completeness [%]	81.0	88.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.5	298	0.17M Ammonium Sulfate, 0.085M Sodium Cacodylate, 25.5% PEG 8000, 15% v/v Glycerol anhydrous, pH 6.5, EVAPORATION, temperature 298 K