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

Capillary crystallization and molecular-replacement solution of haemoglobin II from the clam Lucina pectinata
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DOI:
10.1107/s1744309106002648
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发表时间:
2006-03-01
影响因子:
0.9
通讯作者:
García-Ruiz, JM
García-Ruiz, JM
中科院分区:
生物学4区
文献类型:
--
作者:
Gavira, JA;de Jesus, W;García-Ruiz, JM

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血红蛋白II是存在于居住在加勒比海沿岸的Lucina pectinata软体动物细胞质中的三种血红蛋白之一。使用从其天然来源纯化的HBII,使用具有0.2mm内径的毛细管的反向扩散方法进行结晶筛选。在0.1%(w/v)琼脂糖存在下生长适合数据收集和结构测定的HbII晶体,以提高其质量。晶体属于四面体空间群P4(2)2(1)2,晶胞参数a = B = 73.92,c = 152.35埃,衍射X射线分辨率优于2.0埃。不对称单元是同二聚体,其相应的马修斯系数(V-M)为3.15埃(3)Da(-1),溶剂含量为61体积%。
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 angstrom, and diffracted X-rays to a resolution of better than 2.0 A. The asymmetric unit is a homodimer with a corresponding Matthews coefficient (V-M) of 3.15 angstrom(3) Da(-1) and a solvent content of 61% by volume.