6HMZ

Crystal Structure of a Single-Domain Cyclophilin from Brassica napus Phloem Sap

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P14 (MX2)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-06-08
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0332
Spacegroup name	I 41 2 2
Unit cell lengths	86.580, 86.580, 119.520
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	70.120 - 1.980
R-factor	0.1856
Rwork	0.184
R-free	0.22310
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jjm
RMSD bond length	0.018
RMSD bond angle	2.011
Data reduction software	iMOSFLM (7.1.1)
Data scaling software	SCALA (3.3.22)
Phasing software	MOLREP (11.1.00)
Refinement software	REFMAC (5.8.0103)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	70.120	70.120	2.080
High resolution limit [Å]	1.977	6.250	1.980
Rmerge		0.034	0.466
Rmeas	0.112	0.038	0.513
Rpim	0.046	0.017	0.210
Number of reflections	16197	574	2330
<I/σ(I)>	9.2	11.3	1.6
Completeness [%]	99.8	98.3	100
Redundancy	5.6	5.2	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	The protein concentration was adjusted to 10 mg/ml. The protein solution was supplemented with cyclosporin A at a molar ratio of 2:1 and mixed with the reservoir solution containing 2.4 M sodium malonate, pH 7.0.