1FF0

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	1999-10-08
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	51.240, 57.820, 61.450
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.850
R-factor	0.201 *
Rwork	0.201
R-free	0.23200
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.930
High resolution limit [Å]	1.850	1.850
Rmerge	0.061	0.178
Completeness [%]		99.9

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)