Capillary crystallization and molecular-replacement solution of haemoglobin II from the clam Lucina pectinata.
Haemoglobin II is one of three haemoglobins present in the cytoplasm of the Lucina pectinata mollusc that inhabits the Caribbean coast. Using HBII purified from its natural source, crystallization screening was performed using the counter-diffusion method with capillaries of 0.2 mm inner diameter. Crystals of HbII suitable for data collection and structure determination were grown in the presence of agarose at 0.1%(w/v) in order to improve their quality. The crystals belong to the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 73.92, c = 152.35 A, and diffracted X-rays to a resolution of better than 2.0 A. The asymmetric unit is a homodimer with a corresponding Matthews coefficient (VM) of 3.15 A3 Da(-1) and a solvent content of 61% by volume.
Gavira
José A
JA
Laboratorio de Estudios Cristalográficos-CSIC, P. T. Ciencias de la Salud, Granada, Spain.
de Jesus
Walleska
W
Camara-Artigas
Ana
A
López-Garriga
Juan
J
García-Ruiz
Juan M
JM
D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D006454:Hemoglobins / Q000737:chemistry*
D006454:Hemoglobins