8DCH

Crystal Structure of a highly resistant HIV-1 protease Clinical isolate PR10x with GRL-0519 (tris-tetrahydrofuran as P2 ligand)

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	CCD
Collection date	2017-10-25
Detector	RAYONIX MX300HE
Wavelength(s)	1.0
Spacegroup name	P 41
Unit cell lengths	56.659, 56.659, 78.155
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.250
R-factor	0.1479
Rwork	0.146
R-free	0.18640
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3nu3
RMSD bond length	0.013
RMSD bond angle	0.035
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	SHELX (1997)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.290
High resolution limit [Å]	1.250	1.250
Rmerge	0.080	0.389
Rmeas	0.086	0.078
Rpim	0.033	0.030
Total number of observations	458139
Number of reflections	67583	6718
<I/σ(I)>	20.7	3.1
Completeness [%]	99.4	97
Redundancy	6.8	3.3
CC(1/2)		0.991

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.2	298	Hanging-drop vapor diffusion using equal volumes of protein stock (3.9 mg/mL) and well reservoir solution. Cryoprotected in 30% glycerol. Complex on ice at 1:8 ratio of PR to PI, crystallized in 1 M NaCl and 0.1 M sodium acetate pH 5.2