4L1A

Crystallographic study of multi-drug resistant HIV-1 protease Lopinavir complex: mechanism of drug recognition and resistance

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	298
Detector technology	CCD
Collection date	2008-08-21
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 41
Unit cell lengths	43.828, 43.828, 101.805
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.810 - 1.900
R-factor	0.2006
Rwork	0.197
R-free	0.26003
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.815
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall
Low resolution limit [Å]	43.810
High resolution limit [Å]	1.900
Number of reflections	14375

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6	298	The hanging drop vapor diffusion method was used to form the bipyramidal crystals of the MDR 769 protease. Using a grid screen consisting of sodium chloride (0.7 to 1.4 M) and MES-HEPES buffer (pH 5.5 to 8.1), the HIV-1 protease substrate complex crystals formed overnight at 22 C. Routinely, 0.2 mm crystals, in the longest dimension, were obtained after 14 days of incubation. In each well, there were two droplets, containing 1 lL of protease substrate mixture, 1 lL of reservoir solution and 2 lL of protease substrate mixture, 1 lL of reservoir solution, respectively, 07 mL of well solution., VAPOR DIFFUSION, HANGING DROP, temperature 298K