1KTR

Crystal Structure of the Anti-His Tag Antibody 3D5 Single-Chain Fragment (scFv) in Complex with a Oligohistidine peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-10-02
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.873
Spacegroup name	P 32 2 1
Unit cell lengths	106.510, 106.510, 92.800
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.700
R-factor	0.1904 *
Rwork	0.190
R-free	0.22200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	VL: PDB ENTRY 1TET VH: PDB ENTRY 1PSK
RMSD bond length	0.005
RMSD bond angle	1.317 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.116	0.537
Total number of observations	128480 *
Number of reflections	16996
<I/σ(I)>	16.6	4.4
Completeness [%]	99.0	99.8
Redundancy	7.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.4	4 *	PEG 8000, magnesium acetate, MES, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.8 (mg/ml)
2	1	reservoir	MES	0.1 (M)	pH6.4
3	1	reservoir	magnesium acetate	0.2 (M)
4	1	reservoir	PEG8000	20 (%(w/v))
5	1	reservoir		0.02 (%(w/v))