3MGU

Structure of S. cerevisiae Tpa1 protein, a proline hydroxylase modifying ribosomal protein Rps23

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-06
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9796, 0.9794, 0.9843
Spacegroup name	C 2 2 21
Unit cell lengths	81.180, 104.840, 205.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.920 - 2.800
R-factor	0.2424
Rwork	0.239
R-free	0.29640
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	1.077
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.700	2.900
High resolution limit [Å]	2.800	2.800
Number of reflections	22109
<I/σ(I)>	6.76
Completeness [%]	97.0	92.5
Redundancy	3.58	3.64

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	0.1M Hepes pH7.5, 44% methylpentanediol, 0.1M Mg(NO3)2, VAPOR DIFFUSION, SITTING DROP, temperature 291K