1OHQ

Crystal structure of HEL4, a soluble human VH antibody domain resistant to aggregation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF
Synchrotron site	ESRF
Temperature [K]	100
Collection date	2002-09-15
Spacegroup name	I 41 2 2
Unit cell lengths	76.121, 76.121, 187.069
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	70.000 - 2.000
R-factor	0.182
Rwork	0.182
R-free	0.25600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fgv
RMSD bond length	0.007 *
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	70.000	2.110
High resolution limit [Å]	2.000	2.000
Rmerge	0.143 *	0.667 *
Number of reflections	19067
<I/σ(I)>	4.3	2.2
Completeness [%]	99.7 *	96 *
Redundancy	7.0 *	6.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.2 *		pH 6.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	22.3 (mg/ml)
2	1	reservoir	HEPES	0.1 (M)	pH7.2
3	1	reservoir		1.6 (M)
4	1	reservoir	glycerol	6 (%(v/v))