9B02

nnhA C357A catalytic mutant in tris buffer

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Synchrotron site	Australian Synchrotron
Beamline	MX1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-03-01
Detector	DECTRIS EIGER R 4M
Wavelength(s)	0.953700
Spacegroup name	H 3 2
Unit cell lengths	206.091, 206.091, 69.310
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.300 - 1.970
Rwork	0.165
R-free	0.19790
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.438
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.300	2.010
High resolution limit [Å]	1.970	1.970
Rmerge	0.178	0.909
Rpim	0.055	0.289
Number of reflections	39795	2711
<I/σ(I)>	10.9	2.8
Completeness [%]	99.8
Redundancy	11.3
CC(1/2)	0.996	0.862

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	293	Protein was at 2.5 mg/mL in tris pH 7.0 buffer. The drops were 200 nL plus 200 nL and incubated at 20 C. The reservoir was 21.7% polyacrylic acid 5100, 15 mM MgCl2 and 100 mM HEPES pH 7.2