2QC7

Crystal structure of the protein-disulfide isomerase related chaperone ERp29

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	180
Detector technology	CCD
Collection date	2003-05-21
Detector	MAR CCD 130 mm
Wavelength(s)	0.96676
Spacegroup name	P 1 2 1
Unit cell lengths	58.044, 68.025, 70.088
Unit cell angles	90.00, 107.46, 90.00

Refinement procedure

Resolution	28.980 - 2.900
R-factor	0.265
Rwork	0.265
R-free	0.27900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ovn
RMSD bond length	0.015
RMSD bond angle	1.597
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	28.981	29.980	3.060
High resolution limit [Å]	2.900	9.170	2.900
Rmerge	0.075	0.034	0.599
Total number of observations		2091	10055
Number of reflections	11070
<I/σ(I)>	7.3	16.2	1.3
Completeness [%]	94.6	96.5	100
Redundancy	5.8	5.4	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and 18-20% (w/v) PEG 2000 monomethyl ether. Crystals of about 0.1 mm in size grew in two days. , VAPOR DIFFUSION, HANGING DROP, temperature 277K