2AVM

Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, AND G73S

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	95
Detector technology	CCD
Collection date	2003-03-05
Detector	MAR CCD 165 mm
Wavelength(s)	0.97105
Spacegroup name	P 21 21 2
Unit cell lengths	58.196, 85.893, 46.547
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.100
R-factor	0.104
Rwork	0.106
R-free	0.13200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daz
RMSD bond length	0.017
RMSD bond angle	0.035
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.140
High resolution limit [Å]	1.100	1.100
Rmerge	0.068	0.120
Number of reflections	90988
<I/σ(I)>	25.24	9.9
Completeness [%]	95.9	84
Redundancy	5.5	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8	295	CITRATE/PHOSPHATE BUFFER, PH 5.8,SATURATED AMMONIUM SULPHATE, 5-10%,DMSO 13%, pH 5.80, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K