6VIM

P. putida mandelate racemase co-crystallized with phenylboronic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2019-04-06
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	228.988, 150.356, 150.275
Unit cell angles	90.00, 129.25, 90.00

Refinement procedure

Resolution	116.370 - 2.000
R-factor	0.1602
Rwork	0.158
R-free	0.19830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uxk
RMSD bond length	0.006
RMSD bond angle	0.757
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHASER
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	116.570	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.116	0.597
Number of reflections	262707	26100
<I/σ(I)>	9.2	2.3
Completeness [%]	99.7	99.5
Redundancy	3.8	3.8
CC(1/2)	0.995	0.782

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	294	The reservoir solution consisted of PEG 4000 (10% w/v) and Bis-Tris Propane (BTP; 50 mM, pH 7.0). The protein solution consisted of 6 mg/mL P. putida MR, 1.0 mM phenylboronic acid, 3.3 mM MgCl2, and 50 mM HEPES buffer (pH 7.5). The protein solution and reservoir solution were mixed in a 1:1 ratio to a final volume of 10 uL