9G3Q

Chitinase-like protein AgBR1 from Aedes aegypti

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-03-06
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.9795
Spacegroup name	P 1 21 1
Unit cell lengths	50.432, 77.191, 51.116
Unit cell angles	90.00, 104.84, 90.00

Refinement procedure

Resolution	49.410 - 1.200
R-factor	0.1493
Rwork	0.148
R-free	0.17960
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.039
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHENIX
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.410	1.328
High resolution limit [Å]	1.200	1.204
Rmerge	0.044	0.744
Rmeas	0.048	0.829
Rpim	0.018	0.355
Number of reflections	81290	4065
<I/σ(I)>	15.9	1.525
Completeness [%]	93.5	51.34
Redundancy	6.68	4.98
CC(1/2)	0.999	0.731

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	291.15	Thawed AgBR1 protein was desalted with 150 mM NaCl, 50 mM Tris, pH 7.4 buffer using Micro Bio-Spin columns (Biorad) to eliminate glycerol. The measured nanodrop absorbance was 8.7 mg/mL. 75 nL of protein were mixed with 150 nL of crystallization reservoir buffer contaning 0.1 M MMT, 25% PEG 1,500 from PACT Premier.