4JCI

Crystal structure of csal_2705, a putative hydroxyproline epimerase from CHROMOHALOBACTER SALEXIGENS (TARGET EFI-506486), SPACE GROUP P212121, unliganded

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	2013-02-14
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	48.095, 54.455, 253.040
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	23.940 - 1.700
R-factor	0.171
Rwork	0.169
R-free	0.20500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2azp
RMSD bond length	0.011
RMSD bond angle	1.332
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	250.000	1.790
High resolution limit [Å]	1.700	1.700
Rmerge	0.073	0.644
Number of reflections	72128
<I/σ(I)>	17.5	3.3
Completeness [%]	97.0	94
Redundancy	9.3	7.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		4.8	298	Protein (15 mM Hepes pH 8.0, 150 mM NaCl, 5% glycerol, 10 mM PYRROLE-2-CARBOXYLATE), Reservoir (0.2 M di-Ammonium Citrate pH 5.0, 20 %(w/v) PEG 3350); Soak 2 minutes in (Reservoir + 20% Glycerol), sitting drop vapor diffuction, temperature 298K