1NAK

IGG1 FAB FRAGMENT (83.1) COMPLEX WITH 16-RESIDUE PEPTIDE (RESIDUES 304-321 OF HIV-1 GP120 (MN ISOLATE))

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2000-06-16
Detector	CUSTOM-MADE
Wavelength(s)	1.033
Spacegroup name	P 1 21 1
Unit cell lengths	60.511, 122.597, 69.464
Unit cell angles	90.00, 108.54, 90.00

Refinement procedure

Resolution	48.200 * - 2.570
Rwork	0.288
R-free	0.32600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1acy
RMSD bond length	0.007
RMSD bond angle	26.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.200	2.660
High resolution limit [Å]	2.570	2.570
Rmerge	0.115 *	0.394 *
Total number of observations	87725 *
Number of reflections	29751
<I/σ(I)>	9.4	2.1
Completeness [%]	96.5	80
Redundancy	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	298	1.6M Na/K phosphate, 5% isopropanol, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298.K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15.0 (mg/ml)
2	1	reservoir	sodium potassium phosphate	1.6 (M)
3	1	reservoir	isopropanol	5 (%)	pH6.0