1A9M

G48H MUTANT OF HIV-1 PROTEASE IN COMPLEX WITH A PEPTIDIC INHIBITOR U-89360E

Experimental procedure

Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1996-04
Detector	SIEMENS
Spacegroup name	I 2 2 2
Unit cell lengths	58.500, 88.200, 94.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.185
Rwork	0.185
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gno
RMSD bond length	0.013
RMSD bond angle	28.500 *
Data reduction software	SAINT
Data scaling software	SAINT
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.073 *	0.320 *
Total number of observations	25380 *
Number of reflections	8697
<I/σ(I)>	15	3
Completeness [%]	78.0	52.6
Redundancy	3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.8		THE PROTEIN SOLUTION CONTAINED 6.5 MG/ML MUTANT HIV-1 PROTEASE IN 20 MM SODIUM ACETATE, 1 MM DITHIOTHREITOL, PH 5.5, WITH A 10-FOLD MOLAR EXCESS OF INHIBITOR. THE RESERVOIR SOLUTIONS FOR THE VAPOR DIFFUSION CONTAINED 10% DIMETHYLSULFOXIDE, 30 MM B-MERCAPTOETHANOL AND 4% 2-PROPANOL IN ADDITION TO THE PRECIPITANT. THE MOST FAVORABLE CRYSTALLIZATION CONDITIONS WERE 42% SATURATED AMMONIUM SULFATE, PH 6.8., vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.5 (mg/ml)
2	1	drop	sodium acetate	20 (mM)
3	1	drop	dithiothreitol	1 (mM)
4	1	drop	inhibitor		10-fold molar excess
5	1	reservoir	dimethylsulfoxide	10 (%)
6	1	reservoir	beta-mercaptoethanol	30 (mM)
7	1	reservoir	2-propanol	4 (%)
8	1	reservoir	ammonium sulfate	42 (%sat)