9B01

Catalytic mutant C357A nnhA in CHES 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	206.124, 206.124, 68.215
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	48.000 - 1.990
Rwork	0.146
R-free	0.17380
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.598
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.000	2.040
High resolution limit [Å]	1.990	1.990
Rmerge	0.231	1.011
Rpim	0.072	0.322
Number of reflections	37832	2570
<I/σ(I)>	9.7	2.7
Completeness [%]	99.9	98.3
Redundancy	11.3	10.6
CC(1/2)	0.993	0.830

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	293	Protein was at 2.5 mg/mL in CHES buffer at pH 9.0 and was set up in 200 nL plus 200 nL drops at 20 C. The reservoir was 21.2% polyacrylic acid 5100, 30 mM MgCl2 and 100 mM HEPES at pH 7.2