2P3C

Crystal Structure of the subtype F wild type HIV protease complexed with TL-3 inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE D03B-MX1
Synchrotron site	LNLS
Beamline	D03B-MX1
Temperature [K]	100
Detector technology	CCD
Detector	MAR CCD 165 mm
Spacegroup name	P 61
Unit cell lengths	61.425, 61.425, 80.892
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.270 - 2.100
R-factor	0.201
Rwork	0.194
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Crystal Structure of the multi-drug resistant mutant subtype B HIV protease complexed with TL-3 inhibitor
RMSD bond length	0.013
RMSD bond angle	1.593
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.2.0003)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	53.225	32.210	2.210
High resolution limit [Å]	2.100	6.640	2.100
Rmerge	0.046	0.026	0.318
Total number of observations		800	3638
Number of reflections	10162
<I/σ(I)>	10.8	16.9	2.1
Completeness [%]	99.7	94.2	99.8
Redundancy	2.5	2.6	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.2	291	0.8M ammonium sulfate, 0.1M sodium cacodylate. The crystals nucleated at 277K and were transfered to 291K for further growth. The protein to well proportion was 2:1, pH 6.2, VAPOR DIFFUSION, HANGING DROP
1	VAPOR DIFFUSION, HANGING DROP	6.2	291	0.8M ammonium sulfate, 0.1M sodium cacodylate. The crystals nucleated at 277K and were transfered to 291K for further growth. The protein to well proportion was 2:1, pH 6.2, VAPOR DIFFUSION, HANGING DROP