Auracyanin B structure in space group P6(5).
The structure of auracyanin B, a 'blue' copper protein produced by Chloroflexus aurantiacus, has previously been solved and refined in the hexagonal space group P6(4)22 with a single molecule in the asymmetric unit. The protein has now been crystallized in space group P6(5), with unit-cell parameters a = b = 115.9, c = 108.2 A. In the new crystal form, the asymmetric unit contains four protein molecules. The structure has been solved by molecular replacement and refined at 1.9 A resolution. The final residuals are R = 19.2% and R(free) = 21.9%. In relation to the earlier crystal structure, the doubling of the unit-cell volume and the lower symmetry are explained by small rotations of the molecules with respect to one another.
Lee
Mihwa
M
School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
Maher
Megan J
MJ
Freeman
Hans C
HC
Guss
J Mitchell
JM
D001426:Bacterial Proteins / Q000737:chemistry*; D041861:Chloroflexus / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D008667:Metalloproteins / Q000737:chemistry*; D015394:Molecular Structure
D001426:Bacterial Proteins; D008667:Metalloproteins; C073757:auracyanin B-1 protein, bacteria