High-Resolution Modeling of Protein Structures Based on Flexible Fitting of Low-Resolution Structural Data

2014 ◽  
pp. 267-284 ◽  
Author(s):  
Wenjun Zheng ◽  
Mustafa Tekpinar
Keyword(s):  
High Resolution ◽  
Protein Structures ◽  
Structural Data ◽  
Low Resolution

scholarly journals PyXlinkViewer: a flexible tool for visualisation of protein chemical crosslinking data within the PyMOL molecular graphics system

2020 ◽  
Author(s):  
Bob Schiffrin ◽  
Sheena. E. Radford ◽  
David. J. Brockwell ◽  
Antonio N. Calabrese
Keyword(s):  
High Resolution ◽  
Protein Structures ◽  
Structural Models ◽  
Structural Data ◽  
Chemical Crosslinking ◽  
Molecular Graphics ◽  
Flexible Tool ◽  
Dead End ◽  
Spacer Arm ◽  
User Friendly

AbstractChemical crosslinking-mass spectrometry (XL-MS) is a valuable technique for gaining insights into protein structure and the organization of macromolecular complexes. XL-MS data yields inter-residue restraints that can be compared with high-resolution structural data. Distances greater than the crosslinker spacer-arm can reveal lowly-populated “excited” states of proteins/protein assemblies, or crosslinks can be used as restraints to generate structural models in the absence of structural data. Despite increasing uptake of XL-MS, there are few tools to enable rapid and facile mapping of XL-MS data onto high-resolution structures or structural models. PyXlinkViewer is a user-friendly plugin for PyMOL v2 that maps intra-protein, inter-protein and dead-end crosslinks onto protein structures/models and automates the calculation of inter-residue distances for the detected crosslinks. This enables rapid visualisation of XL-MS data, assessment of whether a set of detected crosslinks is congruent with structural data, and easy production of high-quality images for publication.

scholarly journals QAEmap: A Novel Local Quality Assessment Method for Protein Crystal Structures Using Machine Learning

2021 ◽  
Author(s):  
Ikuko Miyaguchi ◽  
Miwa Sato ◽  
Akiko Kashima ◽  
Hiroyuki Nakagawa ◽  
Yuichi Kokabu ◽  
...  
Keyword(s):  
High Resolution ◽  
Quality Assessment ◽  
Electron Density ◽  
Protein Structures ◽  
Assessment Method ◽  
Protein Crystal ◽  
Low Resolution ◽  
Density Maps ◽  
Density Map ◽  
Electron Density Map

Abstract Low-resolution electron density maps can pose a major obstacle in the determination and use of protein structures. Herein, we describe a novel method, quality assessment based on an electron density map (QAEmap), that evaluates local protein structures determined by X-ray crystallography and corrects structural errors using low-resolution maps. QAEmap uses a three-dimensional deep convolutional neural network with electron density maps and their corresponding coordinates as input and predicts the correlation between the local structure and the putative high-resolution experimental electron density map. This estimates how well the structure fits the high-resolution map. Further, we propose that this method may be applied to evaluate ligand binding, which can be difficult to determine at low resolution.

High-resolution X-ray crystal structure of bovine H-protein at 0.88 Å resolution

2010 ◽  
Vol 66 (6) ◽  
pp. 698-708 ◽  
Author(s):  
Akifumi Higashiura ◽  
Takeshi Kurakane ◽  
Makoto Matsuda ◽  
Mamoru Suzuki ◽  
Koji Inaka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Protein Structures ◽  
Data Sets ◽  
Low Resolution ◽  
Data Set ◽  
X Ray ◽  
H Protein ◽  
Resolution Structure

Recent technical improvements in macromolecular X-ray crystallography have significantly improved the resolution limit of protein structures. However, examples of high-resolution structure determination are still limited. In this study, the X-ray crystal structure of bovine H-protein, a component of the glycine cleavage system, was determined at 0.88 Å resolution. This is the first ultrahigh-resolution structure of an H-protein. The data were collected using synchrotron radiation. Because of limitations of the hardware, especially the dynamic range of the CCD detector, three data sets (high-, medium- and low-resolution data sets) were measured in order to obtain a complete set of data. To improve the quality of the merged data, the reference data set was optimized for merging and the merged data were assessed by comparing merging statistics andRfactors against the final model and the number of visualized H atoms. In addition, the advantages of merging three data sets were evaluated. The omission of low-resolution reflections had an adverse effect on visualization of H atoms in hydrogen-omit maps. Visualization of hydrogen electron density is a good indicator for assessing the quality of high-resolution X-ray diffraction data.

Tubulin structure at intermediate resolution

1995 ◽  
Vol 53 ◽  
pp. 852-853
Author(s):  
K. H. Downing ◽  
S. G. Wolf ◽  
E. Nogales
Keyword(s):  
High Resolution ◽  
Structural Data ◽  
Therapeutic Drug ◽  
Zinc Ions ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray ◽  
Negative Stain ◽  
Functional Mechanisms ◽  
Tubulin Structure

Microtubules are involved in a host of critical cell activities, many of which involve transport of organelles through the cell. Different sets of microtubules appear to form during the cell cycle for different functions. Knowledge of the structure of tubulin will be necessary in order to understand the various functional mechanisms of microtubule assemble, disassembly, and interaction with other molecules, but tubulin has so far resisted crystallization for x-ray diffraction studies. Fortuitously, in the presence of zinc ions, tubulin also forms two-dimensional, crystalline sheets that are ideally suited for study by electron microscopy. We have refined procedures for forming the sheets and preparing them for EM, and have been able to obtain high-resolution structural data that sheds light on the formation and stabilization of microtubules, and even the interaction with a therapeutic drug.Tubulin sheets had been extensively studied in negative stain, demonstrating that the same protofilament structure was formed in the sheets and microtubules. For high resolution studies, we have found that the sheets embedded in either glucose or tannin diffract to around 3 Å.

HRTEM study of valleriite, a hydroxide-bearing copper sulfide

1990 ◽  
Vol 48 (4) ◽  
pp. 462-463
Author(s):  
S. Wang ◽  
P. R. Buseck
Keyword(s):  
Electron Microscope ◽  
High Resolution ◽  
Copper Sulfide ◽  
Carbonaceous Chondrite ◽  
Structural Data ◽  
Basic Structure ◽  
Long Period ◽  
Selected Area Electron Diffraction ◽  
Transmission Electron ◽  
Wavy Structure

Valleriite is an unusual mineral, consisting of intergrowths of sulfide layers (corresponding in structure to the mineral smythite - Fe9S11) and hydroxide layers (corresponding to brucite - Mg(OH2)). It has a composition of approximately 1.526[Mg.68Al.32(OH)2].[Fe1.07Cu.93S2] and consists of two interpenetrating lattices, each of which retains its individual structural and diffraction characteristics parallel to the layering. The valleriite structure is related to that of tochilinite, an unusual iron-rich mineral that is of considerable interest for the origin of certain carbonaceous chondrite meteorites and to those of franckeite and cylindrite, two minerals that are of interest because of their unique morphological and crystallographic properties, e.g., the distinctive curved form of cylindrite and the perfect mica-like cleavage with unusual striations and the long-period wavy structure of franckeite.Our selected-area electron diffraction (SAED) patterns and high-resolution transmission electron microscope (HRTEM) images of valleriite provide new structural data. A basic structure and a new superstructure have been observed.

scholarly journals Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

2021 ◽  
Vol 22 (13) ◽  
pp. 6709
Author(s):  
Xiao-Xuan Shi ◽  
Peng-Ye Wang ◽  
Hong Chen ◽  
Ping Xie
Keyword(s):  
Molecular Dynamics ◽  
High Resolution ◽  
Binding Energy ◽  
Molecular Dynamics Simulations ◽  
Conformational Changes ◽  
Weak Interactions ◽  
Molecular Motor ◽  
Structural Data ◽  
Calculated Binding Energy ◽  
Dynamics Simulations

The transition between strong and weak interactions of the kinesin head with the microtubule, which is regulated by the change of the nucleotide state of the head, is indispensable for the processive motion of the kinesin molecular motor on the microtubule. Here, using all-atom molecular dynamics simulations, the interactions between the kinesin head and tubulin are studied on the basis of the available high-resolution structural data. We found that the strong interaction can induce rapid large conformational changes of the tubulin, whereas the weak interaction cannot. Furthermore, we found that the large conformational changes of the tubulin have a significant effect on the interaction of the tubulin with the head in the weak-microtubule-binding ADP state. The calculated binding energy of the ADP-bound head to the tubulin with the large conformational changes is only about half that of the tubulin without the conformational changes.

scholarly journals Multimodal Low Resolution Face and Frontal Gait Recognition from Surveillance Video

Electronics ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1013
Author(s):  
Sayan Maity ◽  
Mohamed Abdel-Mottaleb ◽  
Shihab S. Asfour
Keyword(s):  
Face Recognition ◽  
High Resolution ◽  
Gait Cycle ◽  
Gait Recognition ◽  
Recognition System ◽  
Multimodal Fusion ◽  
Surveillance Video ◽  
Low Resolution ◽  
Model Free ◽  
Face Images

Biometric identification using surveillance video has attracted the attention of many researchers as it can be applicable not only for robust identification but also personalized activity monitoring. In this paper, we present a novel multimodal recognition system that extracts frontal gait and low-resolution face images from frontal walking surveillance video clips to perform efficient biometric recognition. The proposed study addresses two important issues in surveillance video that did not receive appropriate attention in the past. First, it consolidates the model-free and model-based gait feature extraction approaches to perform robust gait recognition only using the frontal view. Second, it uses a low-resolution face recognition approach which can be trained and tested using low-resolution face information. This eliminates the need for obtaining high-resolution face images to create the gallery, which is required in the majority of low-resolution face recognition techniques. Moreover, the classification accuracy on high-resolution face images is considerably higher. Previous studies on frontal gait recognition incorporate assumptions to approximate the average gait cycle. However, we quantify the gait cycle precisely for each subject using only the frontal gait information. The approaches available in the literature use the high resolution images obtained in a controlled environment to train the recognition system. However, in our proposed system we train the recognition algorithm using the low-resolution face images captured in the unconstrained environment. The proposed system has two components, one is responsible for performing frontal gait recognition and one is responsible for low-resolution face recognition. Later, score level fusion is performed to fuse the results of the frontal gait recognition and the low-resolution face recognition. Experiments conducted on the Face and Ocular Challenge Series (FOCS) dataset resulted in a 93.5% Rank-1 for frontal gait recognition and 82.92% Rank-1 for low-resolution face recognition, respectively. The score level multimodal fusion resulted in 95.9% Rank-1 recognition, which demonstrates the superiority and robustness of the proposed approach.

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