1LW0

CRYSTAL STRUCTURE OF T215Y MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH NEVIRAPINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID2
Synchrotron site	ESRF
Beamline	ID2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-06-27
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.9903
Spacegroup name	P 21 21 21
Unit cell lengths	139.700, 115.000, 65.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.800
R-factor	0.209 *
Rwork	0.219
R-free	0.30200 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.710 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.061
Total number of observations	91111 *
Number of reflections	25400	2107 *
<I/σ(I)>	13.8	1.6
Completeness [%]	93.2	78.5
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	4 *	Stammers, D.K., (1994) J.Mol.Biol., 242, 586. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	26 (mg/ml)
2	1	drop	PEG3400	6 (%(w/v))
3	1	reservoir	PEG3400	6 (%(w/v))
4	1	drop	citrate/phosphate