1FEJ

STRUCTURAL IMPLICATIONS OF DRUG RESISTANT MUTANTS OF HIV-1 PROTEASE: HIGH RESOLUTION CRYSTAL STRUCTURES OF THE MUTANT PROTEASE/SUBSTRATE ANALOG COMPLEXES

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	90
Detector technology	CCD
Collection date	1999-03-14
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	51.230, 58.050, 61.080
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.780
R-factor	0.215 *
Rwork	0.215
R-free	0.28500
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.860
High resolution limit [Å]	1.700	1.780
Rmerge	0.067

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	CITRATE/PHOSPHATE BUFFER 0.05M, DTT 10MM, DMSO 10%, SATURATED AMMONIUM SULPHATE 25-50%, PROTEIN 2-5 MG/ML, pH 5.0-6.5. VAPOR DIFFUSION, HANGING DROP at 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	citrate	0.25 (M)
2	1	reservoir	phosphate	0.5 (M)
3	1	reservoir	DMSO	10 (%)
4	1	reservoir	ammonium sulfate	20-50 (%sat)
5	1	drop	protein	2-5 (mg/ml)