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Title: Capillary crystallization and molecular-replacement solution of haemoglobin II from the clam Lucina pectinata

Journal Article · · Acta Crystallographica. Section F
 [1];  [2]; ;  [3];  [1]
  1. Laboratorio de Estudios Cristalográficos-CSIC, P. T. Ciencias de la Salud, Granada (Spain)
  2. Departamento de Quimica, PO Box 9019, Universidad de Puerto Rico, Recinto de Mayaguez, Mayaguez PR 00681 (Puerto Rico)
  3. Departamento Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento, Almería 04120 (Spain)

The haemoglobin II from the clam L. pectinata has been crystallized using counter-diffusion in single capillary in the presence of agarose to improve crystal quality. Initial phases have been obtained by molecular replacement. 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{sub 2}2{sub 1}2, with unit-cell parameters a = b = 73.92, c = 152.35 Å, and diffracted X-rays to a resolution of better than 2.0 Å. The asymmetric unit is a homodimer with a corresponding Matthews coefficient (V{sub M}) of 3.15 Å{sup 3} Da{sup −1} and a solvent content of 61% by volume.

OSTI ID:
22356306
Journal Information:
Acta Crystallographica. Section F, Vol. 62, Issue Pt 3; Other Information: PMCID: PMC2197196; PMID: 16511300; PUBLISHER-ID: pu5126; OAI: oai:pubmedcentral.nih.gov:2197196; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English