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Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide

机译:人主要组织相容性抗原HLA-B * 2703与病毒肽和自身肽复合的纯化,结晶和初步X射线衍射分析

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摘要

The product of the human leukocyte antigen (HLA) gene HLA-B*2703 differs from that of the prototypical subtype HLA-B*2705 by a single amino acid at heavy-chain residue 59 that is involved in anchoring the peptide N-terminus within the A pocket of the molecule. Two B*2703–peptide complexes were crystallized using the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant. A pocket of the molecule, two HLA-B*2703–peptide complexes were crystallized and data sets were collected to high resolution using synchrotron radiation.
机译:人类白细胞抗原(HLA)基因HLA-B * 2703的产物与原型亚型HLA-B * 2705的产物的不同之处在于重链残基59上的单个氨基酸,该氨基酸参与将肽N端锚定在分子的口袋。使用PEG 8000作为沉淀剂,采用悬滴蒸汽扩散法结晶了两个B * 2703-肽复合物。分子的一个口袋中,两个HLA-B * 2703-肽复合物结晶,并使用同步加速器辐射将数据集收集到高分辨率。

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