4LB0

Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-proline

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-12
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 42 21 2
Unit cell lengths	178.014, 178.014, 49.735
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.165 - 1.700
R-factor	0.1594
Rwork	0.158
R-free	0.19190
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4k8l
RMSD bond length	0.010
RMSD bond angle	1.320
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	AMoRE
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	125.875	178.014	1.790
High resolution limit [Å]	1.700	5.380	1.700
Rmerge	0.078	0.032	0.745
Total number of observations		39677	99779
Number of reflections	88126
<I/σ(I)>	18.3	21.2	1
Completeness [%]	99.9	98.7	99.9
Redundancy	10.4	13	7.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	Protein (15 mM Bis-Tris, 500 mM NaCl, 10% glycerol, 5 mM DTT, 200 mM 4-OH PROLINE, TEV Treated, Cleavage Unverified); Reservoir (0.1 M NaAcetate, 25% Peg4000, 8% 2-propanol (MCSG4 H2)); Cryoprotection (Reservoir+20% isopropanaol) , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K