8BAL

Niako3494, a bacterial protein structure in glycoside hydrolase family 20

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-04-29
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.9762
Spacegroup name	C 2 2 21
Unit cell lengths	146.987, 254.589, 139.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	73.490 - 2.270
Rwork	0.283
R-free	0.35610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Alphafold
RMSD bond length	0.007
RMSD bond angle	1.613
Data reduction software	xia2
Data scaling software	xia2
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	73.490	2.310
High resolution limit [Å]	2.270	2.270
Number of reflections	120442	5852
<I/σ(I)>	6.3	1.1
Completeness [%]	99.9	99.1
Redundancy	13.9	13.6
CC(1/2)	0.958	0.336

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein stock at 18mg/mL, in the precipitant: 0.1 M MMT buffer (DL-Malic acid, MES monohydrate, Tris base [ratio 1:2:2]), pH 6.0, 25 % w/v PEG 1500, protein to precipitant ratio 1:1, 1 uL drop size, +50 nL 1:10000 diluted seed stock. Cryoprotectant used was made up with 20% PEG400 in 80% mother liquor.