1K2C

Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1999-05-26
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	51.903, 59.510, 61.913
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
Rwork	0.201
R-free	0.29000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daz
RMSD bond length	0.010
RMSD bond angle	1.834
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000 *	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.066	0.171
Number of reflections	8863
<I/σ(I)>	10
Completeness [%]	86.8	89.5
Redundancy	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	20-50% Saturated Ammonium Sulphate, 10% DMSO, 0.25M citrate/0.5M phosphate buffer, VAPOR DIFFUSION, HANGING DROP, temperature 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)	pH5-6.5
3	1	reservoir	DMSO	10 (%)
4	1	reservoir	dithiothreitol	10 (mM)
5	1	reservoir	ammonium sulfate	20-50 (%sat)
6	1	drop	protein	2-10 (mg/ml)