9O9W

Crystal structure of an alpha/beta-hydrolase from Actinoplanes sp. DH11

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL12-2
Synchrotron site	SSRL
Beamline	BL12-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-03-04
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97946
Spacegroup name	P 32 2 1
Unit cell lengths	87.250, 87.250, 148.870
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	37.780 - 1.760
R-factor	0.16278
Rwork	0.161
R-free	0.19853
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.639
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0430)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	37.780	37.780	1.810
High resolution limit [Å]	1.760	7.870	1.760
Rmerge	0.123	0.047	2.614
Rmeas	0.128	0.049	2.713
Number of reflections	65654	824	4785
<I/σ(I)>	13.34
Completeness [%]	100.0
Redundancy	13.5
CC(1/2)	0.999	0.998	0.697

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	30% Precipitant Mix 1, 0.06 M Divalents, Buffer system 1 (pH 6.5) (Morpheus screen)