1K2B

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]	90
Detector technology	CCD
Collection date	1999-10-08
Detector	ADSC QUANTUM 4
Wavelength(s)	1.037
Spacegroup name	P 21 21 21
Unit cell lengths	50.759, 57.541, 60.841
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.700
Rwork	0.215
R-free	0.27500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daz
RMSD bond length	0.011
RMSD bond angle	2.183
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000 *	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.042	0.248
Number of reflections	20000
<I/σ(I)>	10.8	5.1
Completeness [%]	99.0	98.4
Redundancy	4.1

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)