3HBD

Class IV chitinase structure from Picea abies at 1.8A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-02-26
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9998
Spacegroup name	P 21 21 2
Unit cell lengths	67.004, 65.579, 36.481
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.17749
Rwork	0.176
R-free	0.20993
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Homology model of the Picea abies chitinase built on barley seed chitinase (PDB entry 1CNS)
RMSD bond length	0.014
RMSD bond angle	1.267
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.078	0.481
Number of reflections	14815
<I/σ(I)>	13	3.1
Completeness [%]	97.4	88.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	296	20% w/v polyethylene glycol 3000, 0.1M citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K