3F58

IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 12-RESIDUE CYCLIC PEPTIDE (INCLUDING RESIDUES 315-324 OF HIV-1 GP120 (MN ISOLATE); H315S MUTATION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE M18X
Temperature [K]	295
Detector technology	AREA DETECTOR
Collection date	1992-05-01
Detector	SIEMENS
Spacegroup name	P 21 21 2
Unit cell lengths	95.470, 115.460, 49.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.000 - 2.800
R-factor	0.2
Rwork	0.200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	FAB PORTION OF 1ACY
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	X-GEN
Data scaling software	X-GEN
Phasing software	MERLOT
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.800	2.980
High resolution limit [Å]	2.800	2.800
Rmerge	0.072 *	0.218 *
Total number of observations	47266 *
Number of reflections	13951	2259 *
<I/σ(I)>	13.2	1.5
Completeness [%]	98.9	97.7
Redundancy	3.4	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5	22.5 *	pH 5.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	16 (%)
2	1	reservoir	imidazole malate	0.2 (M)
3	1	drop	peptide		2.4 times Fab molar
4	1	drop	Fab	15 (mg/ml)