1OL0

Crystal structure of a camelised human VH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-10-15
Detector	ADSC CCD
Spacegroup name	P 32 2 1
Unit cell lengths	75.300, 75.300, 101.780
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.200 * - 1.800
R-factor	0.15576
Rwork	0.154
R-free	0.18020 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hcv
RMSD bond length	0.017 *
RMSD bond angle	0.038 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.200 *	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.051	0.227
Total number of observations	69437 *
Number of reflections	29910
<I/σ(I)>	17.2	1.5
Completeness [%]	94.9	71.5
Redundancy	2.3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		CRYSTALS GREW FROM 4 MICROLITRE HANGING DROPS FORMED BY MIXING 2 MICROLITERS OF PROTEIN AT A CONCENTRATION OF 5MG/ML WITH 2 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 15-20% (W/V) PEG 8000, 0.4 M AMMONIUM SULPHATE AND 0.1M HEPES AT PH 7.5.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	PEG8000	15-20 (%(w/v))
3	1	reservoir	ammonium sulfate	0.4 (M)
4	1	reservoir	HEPES	0.1 (M)	pH7.5