4MST

Crystal Structure of a putative catalytic domain of a chitinase-like protein (HbCLP1) from Hevea brasiliensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2011-12-02
Detector	PSI PILATUS 6M
Wavelength(s)	0.978570
Spacegroup name	I 1 2 1
Unit cell lengths	111.106, 40.415, 111.854
Unit cell angles	90.00, 96.73, 90.00

Refinement procedure

Resolution	41.658 - 1.927
R-factor	0.1676
Rwork	0.166
R-free	0.20210
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3cql
RMSD bond length	0.011
RMSD bond angle	1.109
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.8.3_1479))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	83.316	41.620	2.060
High resolution limit [Å]	1.927	6.170	1.950
Rmerge	0.088	0.041	0.519
Number of reflections	37443
<I/σ(I)>	14.16	30	4.4
Completeness [%]	99.3	99.8	99.5
Redundancy	6.6	6.5	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	291	7 mg/mL protein, 0.1 M Tris-HCl, pH 8.3, 0.2 M magnesium chloride, 30% PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K