3EBR

Crystal structure of an rmlc-like cupin protein (reut_a0381) from ralstonia eutropha jmp134 at 2.60 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-22
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91837,0.97941,0.97854
Spacegroup name	P 42 2 2
Unit cell lengths	91.157, 91.157, 48.753
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.831 - 2.600
R-factor	0.229
Rwork	0.227
R-free	0.26200
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	1.885
Data reduction software	MOSFLM
Data scaling software	SCALA (3.2.5)
Phasing software	SHARP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	28.831	28.830	2.670
High resolution limit [Å]	2.600	11.630	2.600
Rmerge	0.074	0.054	0.596
Total number of observations		318	2290
Number of reflections	6713
<I/σ(I)>	15.1	28.1	2.2
Completeness [%]	99.9	92.8	100
Redundancy	4.7	3.5	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	60.0% polyethylene glycol 200, 0.1M HEPES pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K