8BEO

Crystal structure of E. coli glyoxylate carboligase mutant I393A with MAP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2009-07-14
Detector	ADSC QUANTUM 210
Wavelength(s)	0.9334
Spacegroup name	P 41 21 2
Unit cell lengths	188.641, 188.641, 246.957
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.350 - 1.960
R-factor	0.177
Rwork	0.176
R-free	0.20400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pan
Data reduction software	XDS (20210120)
Data scaling software	XDS (20210120)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.350	2.060
High resolution limit [Å]	1.960	1.960
Rmerge	0.133	0.957
Number of reflections	277858	13894
<I/σ(I)>	9.83	1.73
Completeness [%]	88.3	33.5
Redundancy	7.19	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	7	296	2-4 ul protein (5-15 mg/ml), 100uM ThDP, 10 uM FAD, 1mM MgCl2, 10mM MAP and 10 mM Q0 were mixed with equal volume of resrvoir solution (0.5% PEG 6000, 0.5 M NaCl and 40 mM DTT). Crystals grew to size of roughly 0.15-0.25 mm in all dimensions.