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巴氏梭菌和棕色固氮菌固氮酶的钼铁蛋白的晶体学性质

Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii.

作者信息

Weininger M S, Mortenson L E

出版信息

Proc Natl Acad Sci U S A. 1982 Jan;79(2):378-80. doi: 10.1073/pnas.79.2.378.

DOI:10.1073/pnas.79.2.378
PMID:6952190
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC345741/
Abstract

Preliminary x-ray diffraction data from single crystals of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii have been obtained. Both protein crystals belong to the P2(1) space group. The MoFe protein crystals from C. pasteurianum and A. vinelandii diffract to angles corresponding to resolutions as great as 2.4 A and 3.0 A, respectively. The cell dimensions of the MoFe protein crystals from the two species have been determined from precession photographs.

摘要

已获得来自巴氏梭菌和棕色固氮菌固氮酶的钼铁蛋白单晶的初步X射线衍射数据。两种蛋白质晶体都属于P2(1)空间群。来自巴氏梭菌和棕色固氮菌的钼铁蛋白晶体分别衍射到对应于高达2.4埃和3.0埃分辨率的角度。已通过进动照片确定了这两个物种的钼铁蛋白晶体的晶胞尺寸。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/4a94efa69038/pnas00441-0180-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/c0c526dbf2eb/pnas00441-0179-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/1049d647f4f6/pnas00441-0179-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/636ae419b474/pnas00441-0179-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/4a94efa69038/pnas00441-0180-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/c0c526dbf2eb/pnas00441-0179-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/1049d647f4f6/pnas00441-0179-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/636ae419b474/pnas00441-0179-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a7/345741/4a94efa69038/pnas00441-0180-a.jpg

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本文引用的文献

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Solvent content of protein crystals.蛋白质晶体的溶剂含量。
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Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the carbon monoxide inhibited state.固氮酶钼铁蛋白组分中的铁硫簇。一氧化碳抑制状态下的电子顺磁共振。
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