3H5B

Crystal structure of wild type HIV-1 protease with novel P1'-ligand GRL-02031

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-06-12
Detector	MAR scanner 300 mm plate
Wavelength(s)	0.8000
Spacegroup name	P 21 21 2
Unit cell lengths	58.111, 86.416, 45.970
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.290
R-factor	0.1436
Rwork	0.142
R-free	0.18130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3djk
RMSD bond length	0.012
RMSD bond angle	0.031
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.340
High resolution limit [Å]	1.290	1.290
Rmerge	0.055	0.491
Number of reflections	54628
<I/σ(I)>	27	2.27
Completeness [%]	92.5	64.3
Redundancy	6.6	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	298	Inhibitor GRL-02031 was dissolved in dimethylsulfoxide (DMSO). Crystals were grown using 1:5 molar ratio of protease (at 3.9 mg/ml) to inhibitor. The reservoir contained 0.1 M citrate phosphate buffer, pH 5.0, 0.35 M NaCl and 4% DMSO. Crystals were mounted on a nylon loop and flash-frozen in liquid nitrogen with a cryoprotectant of 30% v/v glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K