We compare our method with four competing methods in Table 1 of the main paper. We also use the score reported by [5]. We found that the corner-based methods, e.g., HEA T and RoomFormer, fail to reconstruct the correct floorplans and are easily affected by the irregular Heat: Holistic edge attention transformer for structured reconstruction. Real-world perception for embodied agents.

Cryo-electron microscopy (cryo-EM) is an experimental technique for protein structure determination that images an ensemble of macromolecules in near-physiological contexts. While recent advances enable the reconstruction of dynamic conformations of a single biomolecular complex, current methods do not adequately model samples with mixed conformational and compositional heterogeneity. In particular, datasets containing mixtures of multiple proteins require the joint inference of structure, pose, compositional class, and conformational states for 3D reconstruction.

However, both L2 and BL have two deficiencies. First, the noise in the annotation process is not considered in a principled way. L2 and BL make an assumption about per-pixel i.i.d.

DM-Count reduced the error of the state-of-the-art published result by approximately16%.

The annotation noise in crowd counting is not modeled in traditional crowd counting algorithms based on crowd density maps. In this paper, we first model the annotation noise using a random variable with Gaussian distribution, and derive the pdf of the crowd density value for each spatial location in the image. We then approximate the joint distribution of the density values (i.e., the distribution of density maps) with a full covariance multivariate Gaussian density, and derive a low-rank approximate for tractable implementation. We use our loss function to train a crowd density map estimator and achieve state-of-the-art performance on three large-scale crowd counting datasets, which confirms its effectiveness. Examination of the predictions of the trained model shows that it can correctly predict the locations of people in spite of the noisy training data, which demonstrates the robustness of our loss function to annotation noise.

In crowd counting, each training image contains multiple people, where each person is annotated by a dot. Existing crowd counting methods need to use a Gaussian to smooth each annotated dot or to estimate the likelihood of every pixel given the annotated point. In this paper, we show that imposing Gaussians to annotations hurts generalization performance. Instead, we propose to use Distribution Matching for crowd COUNTing (DM-Count). In DM-Count, we use Optimal Transport (OT) to measure the similarity between the normalized predicted density map and the normalized ground truth density map. To stabilize OT computation, we include a Total Variation loss in our model. We show that the generalization error bound of DM-Count is tighter than that of the Gaussian smoothed methods. In terms of Mean Absolute Error, DM-Count outperforms the previous state-of-the-art methods by a large margin on two large-scale counting datasets, UCF-QNRF and NWPU, and achieves the state-of-the-art results on the ShanghaiTech and UCF-CC50 datasets. DM-Count reduced the error of the state-of-the-art published result by approximately 16%.

Protein structure prediction models are now capable of generating accurate 3D structural hypotheses from sequence alone. However, they routinely fail to capture the conformational diversity of dynamic biomolecular complexes, often requiring heuristic MSA subsampling approaches for generating alternative states. In parallel, cryo-electron microscopy (cryo-EM) has emerged as a powerful tool for imaging near-native structural heterogeneity, but is challenged by arduous pipelines to transform raw experimental data into atomic models. Here, we bridge the gap between these modalities, combining cryo-EM density maps with the rich sequence and biophysical priors learned by protein structure prediction models. Our method, CryoBoltz, guides the sampling trajectory of a pretrained biomolecular structure prediction model using both global and local structural constraints derived from density maps, driving predictions towards conformational states consistent with the experimental data. We demonstrate that this flexible yet powerful inference-time approach allows us to build atomic models into heterogeneous cryo-EM maps across a variety of dynamic biomolecular systems including transporters and antibodies. Code is available at https://github.com/ml-struct-bio/cryoboltz .