1K1T

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	95
Detector technology	CCD
Collection date	2000-10-20
Detector	ADSC QUANTUM 4
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	51.256, 58.130, 61.563
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.200
R-factor	0.1957
Rwork	0.196
R-free	0.22700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	0.028
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000 *	1.230
High resolution limit [Å]	1.200	1.200
Rmerge	0.046 *	0.155
Number of reflections	50107
Completeness [%]	86.2	50.3

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)